query: peptidyl t rna is bound to which site

pos: P-site P-site The P-site (for peptidyl) is the second binding site for tRNA in the ribosome. The other two sites are the A-site (aminoacyl), which is the first binding site in the ribosome, and the E-site (exit), is the third and final binding site in the ribosome. During Protein translation, the P-site holds the tRNA which is linked to the growing polypeptide chain. When a stop codon is reached, the peptidyl-tRNA bond of the tRNA located in the P-site is cleaved releasing the newly synthesized protein. During the translocation step of the elongation phase, the mRNA is advanced by one codon,

pos: P-site Prior to peptide bond formation, an aminoacyl-tRNA is bound in the A-site, a peptidyl-tRNA is bound in the P-site, and a deacylated tRNA (ready to exit from the ribosome) is bound to the E-site. Translation moves the tRNA from the A-site through the P- and E-sites, with the exception of the initiator tRNA, which binds directly to the P-site. Recent experiments have reported that protein translation can also initiate from A-site. Using Toeprinting assay, it has been shown that Protein Synthesis initiates from the A-site of the Ribosome (Eukaryotic) in the cricket paralysis virus (CrPV). IGR-IRES (Intragenic regions-internal ribosome entry

pos: P-site peptidyl-tRNA is transferred to the P-site. Chemical modification experiments provided evidence of a hybrid model, where tRNAs can sample a hybrid state of binding during elongation phase (pre-translocation step). These hybrid states of binding are in which acceptor and anti-codon ends of tRNA are in different sites (A, P and E). Using Chemical probing methods, a set of phylogenetically conserved bases in ribosomal RNA where the tRNA binds has been examined and suggested to be directly involved in the binding of tRNA to the prokaryotic ribosome. Correlation of such site specific protected bases in rRNA and occupancy of the A,

pos: Transfer RNA moved to the P/P and E/E sites, the mRNA has also moved over by one codon and the A/T site is vacant, ready for the next round of mRNA decoding. The tRNA bound in the E/E site then leaves the ribosome. The P/I site is actually the first to bind to aminoacyl tRNA, which is delivered by an initiation factor called IF2 in bacteria. However, the existence of the P/I site in eukaryotic or archaeal ribosomes has not yet been confirmed. The P-site protein L27 has been determined by affinity labeling by E. Collatz and A.P. Czernilofsky ("FEBS Lett.", Vol.

pos: EF-Tu the specific amino acid that they are charged with. Messenger RNA (mRNA) carries the genetic information that encodes the primary structure of a protein, and contains codons that code for each amino acid. The ribosome creates the protein chain by following the mRNA code and integrating the amino acid of an aminoacyl-tRNA (also known as a charged tRNA) to the growing polypeptide chain. There are three sites on the ribosome for tRNA binding. These are the aminoacyl/acceptor site (abbreviated A), the peptidyl site (abbreviated P), and the exit site (abbreviated E). The P-site holds the tRNA connected to the polypeptide

pos: P-site P-site The P-site (for peptidyl) is the second binding site for tRNA in the ribosome. The other two sites are the A-site (aminoacyl), which is the first binding site in the ribosome, and the E-site (exit), is the third and final binding site in the ribosome. During Protein translation, the P-site holds the tRNA which is linked to the growing polypeptide chain. When a stop codon is reached, the peptidyl-tRNA bond of the tRNA located in the P-site is cleaved releasing the newly synthesized protein. During the translocation step of the elongation phase, the mRNA is advanced by one codon,

pos: Ribosome P and E. The A-site binds an aminoacyl-tRNA; the P-site binds a peptidyl-tRNA (a tRNA bound to the peptide being synthesized); and the E-site (exit) binds a free tRNA before it exits the ribosome. Protein synthesis begins at a start codon AUG near the 5' end of the mRNA. mRNA binds to the P site of the ribosome first. The ribosome is able to identify the start codon by use of the Shine-Dalgarno sequence of the mRNA in prokaryotes and Kozak box in eukaryotes. Although catalysis of the peptide bond involves the C2 hydroxyl of RNA's P-site adenosine in a

pos: P-site prevent peptide bond formation and/or the translocation of tRNA from the A-site to the P-site on the ribosome that eventually leads to interference with the elongation step and thus the inhibition of protein translation. P-site The P-site (for peptidyl) is the second binding site for tRNA in the ribosome. The other two sites are the A-site (aminoacyl), which is the first binding site in the ribosome, and the E-site (exit), is the third and final binding site in the ribosome. During Protein translation, the P-site holds the tRNA which is linked to the growing polypeptide chain. When a stop codon

neg: Eukaryotic large ribosomal subunit (60S) the left as seen from the subunit interface and L7/L12 on the right). There are three binding sites for tRNA, the A-site, P-site and E-site (see article on protein translation for details). The core of the 60S subunit is formed by the 28S ribosomal RNA (abbreviated 28S rRNA), which is homologous to the prokaryotic 23S rRNA, which also contributes the active site (peptidyl transferase center, PTC) of the ribosome. The rRNA core is decorated with dozens of proteins. In the figure "Crystal Structure of the Eukaryotic 60S Ribosomal Subunit from "T. thermophila"", the ribosomal RNA core is represented as a

neg: Transfer RNA peptide bond to be formed to its attached amino acid. The peptidyl-tRNA, which transfers the growing polypeptide to the aminoacyl-tRNA bound in the A/A site, is bound in the P/P site. Once the peptide bond is formed, the tRNA in the P/P site is deacylated, or has a free 3’ end, and the tRNA in the A/A site carries the growing polypeptide chain. To allow for the next elongation cycle, the tRNAs then move through hybrid A/P and P/E binding sites, before completing the cycle and residing in the P/P and E/E sites. Once the A/A and P/P tRNAs have

neg: 23S ribosomal RNA genes, 23S rRNA genes typically have higher sequence variations including insertions and/or deletions. In general, rRNA has an essential function of peptidyl transferase, the stimulating core of the ribosome plays role in the peptide bond configuration. Both peptidyl-tRNA and aminoacyl-tRNA are important for synthesizing protein and transpeptidation response. However, 23S rRNA positions which are G2252, A2451, U2506, and U2585 have a significant function for tRNA binding in P site of the large ribosomal subunit. These modification nucleotides in site P can inhibit peptidyl-tRNA from binding and also remains U2555 modification intervene with transferring peptidyl-tRNA to puromycin.Furthermore, the chemical modification of

neg: Prokaryotic large ribosomal subunit G-protein factors (assists initiation, elongation, and termination), and helps protein folding after synthesis. An induced-fit mechanism has been revealed for how 50S catalyzes the peptidyl transfer reaction and prevents peptidyl hydrolysis. The amino group of an aminoacyl-tRNA (binds to A site) attacks the carbon of a carbonyl group of a peptidyl-tRNA (binds to P site) and finally yields a peptide extended by one amino acid esterified to the A site tRNA bound to the ribosomal A site and a deacylated tRNA in the P site. When the A site is unoccupied, nucleotide U2620 (E. coli U2585), A2486 (2451) and C2106

neg: Transfer RNA Thus, glutamate tRNA synthetase charges tRNA-glutamine(tRNA-Gln) with glutamate. An amidotransferase then converts the acid side chain of the glutamate to the amide, forming the correctly charged gln-tRNA-Gln. The ribosome has three binding sites for tRNA molecules that span the space between the two ribosomal subunits: the A (aminoacyl), P (peptidyl), and E (exit) sites. In addition, the ribosome has two other sites for tRNA binding that are used during mRNA decoding or during the initiation of protein synthesis. These are the T site (named elongation factor Tu) and I site (initiation). By convention, the tRNA binding sites are denoted with

neg: History of RNA biology scientists had worked to identify which protein(s) within the ribosome were responsible for peptidyl transferase function during translation, because the covalent linking of amino acids represents one of the most central chemical reactions in all of biology. Careful biochemical studies showed that extensively-deproteinized large ribosomal subunits could still catalyze peptide bond formation, thereby implying that the sought-after activity might lie within ribosomal RNA rather than ribosomal proteins. Structural biologists, using X-ray crystallography, localized the peptidyl transferase center of the ribosome to a highly-conserved region of the large subunit ribosomal RNA (rRNA) that is located at the place within the ribosome

neg: Ribosome sites on rat liver ribosomes. Several proteins, including L32/33, L36, L21, L23, L28/29 and L13 were implicated as being at or near the peptidyl transferase center. The ribosomes found in chloroplasts and mitochondria of eukaryotes also consist of large and small subunits bound together with proteins into one 70S particle. These organelles are believed to be descendants of bacteria (see Endosymbiotic theory) and, as such, their ribosomes are similar to those of bacteria. The various ribosomes share a core structure, which is quite similar despite the large differences in size. Much of the RNA is highly organized into various tertiary

neg: 23S ribosomal RNA half of these positions G2251, G2253, A2439, and U2584 can not prevent the tRNA binding. Peptidyl-tRNA of 50s subunits which binds to the P site preserve eight positions of 23S rRNA from chemical modification. On the other hand, 23S rRNA impacts on mutation for cell growth. Mutations A1912G, A1919G and Ψ1917C have a powerful growth phenotypes and they prevent translation while mutation A1916G has a simple growth phenotype and it leads to defect in the 50S subunits. 23S ribosomal RNA The 23S rRNA is a 2904 nt long (in "E. coli") component of the large subunit (50S) of the bacterial/archean

neg: Transfer RNA the ribosome as part of a complex with elongation factor Tu (EF-Tu) or its eukaryotic (eEF-1) or archaeal counterpart. This initial tRNA binding site is called the A/T site. In the A/T site, the A-site half resides in the small ribosomal subunit where the mRNA decoding site is located. The mRNA decoding site is where the mRNA codon is read out during translation. The T-site half resides mainly on the large ribosomal subunit where EF-Tu or eEF-1 interacts with the ribosome. Once mRNA decoding is complete, the aminoacyl-tRNA is bound in the A/A site and is ready for the next

neg: Epitranscriptome is called CeU-Seq, which uses a biotinylated derivative of CMCT. This enables the purification and enrichment of biotinylated transcripts (transcripts modified with pseudouridine) with streptavidin columns, therefore reducing the library size and increasing sensitivity. Other pseudouridine detection methods include site-specific cleavage and radioactive-labeling followed by ligation-assisted extraction and thin-layer chromatography (SCARLET) and mass spectrometry. Ribosomal RNA, or rRNA, forms the nucleic acid component of ribosomes. rRNA modifications take place in and around the peptidyl transferasecenter, the active site of the ribosome. Some modifications include pseudouridines, 2′-O-methylations on backbone sugars, and methylated bases. It is not well known what the biological

neg: 23S ribosomal RNA 23S ribosomal RNA The 23S rRNA is a 2904 nt long (in "E. coli") component of the large subunit (50S) of the bacterial/archean ribosome. The ribosomal peptidyl transferase activity resides in domain V of this rRNA, and this domain is the most common binding site for antibiotics that inhibit translation. A well-known member of this antibiotic class, chloramphenicol, acts by inhibiting peptide bond formation, with recent 3D-structural studies showing two different binding sites depending on the species of ribosome. Linezolid and quinupristin-dalfopristin also bind to the 23S rRNA, and cross-resistance has been demonstrated between these antibiotics. Compared to 16S rRNA

neg: ChiRP-Seq at specific locations on the genome indicates that the RNA of interest had bound to that region of the genome. This helps delineate specific genomic regions that interact with RNA. For example, genomic targets of enhancer RNA which act at a distance from their site of synthesis can be easily evaluated by ChiRP-Seq. ChiRP-Seq ChiRP-Seq (Chromatin Isolation by RNA purification) is a high-throughput sequencing method to discover regions of the genome which are bound by a specific RNA (or by a ribonucleoprotein containing the RNA of interest). Recent studies have shown that a significant proportion of some genomes (including mouse

neg: Regulator gene elements which obstruct the binding of RNA polymerase to the promoter region, thus repressing transcription. In terms of the lac operon, the negative regulator would be the lac repressor which binds to the promoter in the same site that RNA polymerase normally binds. The binding of the lac repressor to RNA polymerase's binding site inhibits the transcription of the lac genes. Only when a corepressor is bound to the lac repressor will the binding site be free for RNA polymerase to carry out transcription of the lac genes. Promoters reside at the beginning of the gene and serve as the

neg: PPIE (gene) β-barrel is composed of eight anti-parallel β-strands and capped by two α-helices at the top and bottom. In addition, the β-turns and loops in the strands contribute to the flexibility of the barrel. In particular, PPIE contains two RNA-binding domains at the N-terminal and a 165-bases long PPIase domain at the C-terminal. The PPIase domain is homologous to PPIA and can be bound and inhibited by CsA. The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of

neg: Ribosomal L28e protein family new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites. About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits. Many of ribosomal proteins, particularly those of the large subunit, are

neg: Nucleic acid tertiary structure as terbium (Tb) are useful experimental tools for studying metal binding to RNA. A metal ion can interact with RNA in multiple ways. An ion can associate diffusely with the RNA backbone, shielding otherwise unfavorable electrostatic interactions. This charge screening is often fulfilled by monovalent ions. Site-bound ions stabilize specific elements of RNA tertiary structure. Site-bound interactions can be further subdivided into two categories depending on whether water mediates the metal binding. “Outer sphere” interactions are mediated by water molecules that surround the metal ion. For example, magnesium hexahydrate interacts with and stabilizes specific RNA tertiary structure motifs via interactions

neg: RNA highly functional regions, such as the peptidyl transferase center and the subunit interface, implying that they are important for normal function. The functional form of single-stranded RNA molecules, just like proteins, frequently requires a specific tertiary structure. The scaffold for this structure is provided by secondary structural elements that are hydrogen bonds within the molecule. This leads to several recognizable "domains" of secondary structure like hairpin loops, bulges, and internal loops. Since RNA is charged, metal ions such as Mg are needed to stabilise many secondary and tertiary structures. The naturally occurring enantiomer of RNA is -RNA composed of -ribonucleotides.

neg: Hypercycle (chemistry) translation. An RNA ligase, in turn, could link various components of quasispecies into one chain, beginning the process of a genome integration. An RNA with a synthase or a synthetase activity could be critical for building compartments and providing building blocks for growing RNA and protein chains as well as other types of molecules. Many examples of this kind of ribozyme are currently known, including a peptidyl transferase ribozyme, a ligase, and a nucleotide synthetase. A transaminoacylator described in 2013 has five nucleotides, which is sufficient for a trans-amino acylation reaction and makes it the smallest ribozyme that has been

neg: Transcription factor II B TFIIB is capable of binding RNA polymerase II both when it is bound to TFIIF and when it is not. Each of the domains in TFIIB interacts with different parts of RNA polymerase II. The amino terminal B ribbon is located on dock domain of RNA polymerase II and extends in to the cleft towards the active site. Extending the B ribbon is the B reader that extends via the RNA exit tunnel to the binding site of the DNA-RNA hybrid and towards the active site. The B linker is the region between the B reader and the B core

neg: Hypercycle (chemistry) discovered. It supports a peptidyl-RNA synthesis that could be a precursor for the contemporary process of linking amino acids to tRNA molecules. An RNA ligase's catalytic domain, consisting of 93 nucleotides, proved to be sufficient to catalyse a linking reaction between two RNA chains. Similarly, an acyltransferase ribozyme 82 nucleotides long was sufficient to perform an acyltransfer reaction. Altogether, the results concerning the RNA ligase's catalytic domain and the acyltransferase ribozyme are in agreement with the estimated upper limit of 100 nucleotides set by the error threshold problem. However, it was hypothesized that even if the putative first RNA-dependent RNA-polymerases

neg: Transducin This binding site on the larger molecular subunit may be immediately adjacent to the T binding site on the γ subunit. Although the traditional mechanism involves activation of PDE by GTP-bound T, GDP-bound T has also been demonstrated to have the ability to activate PDE. Experiments of PDE activation in the dark (without the presence of GTP) show small but reproducible PDE activation. This can be explained by the activation of PDE by free GDP-bound T. PDE γ subunit affinity for GDP-bound T, however, seems to be about 100-fold smaller than for GTP-bound T. The mechanism by which GDP-bound T

neg: Gene of the open reading frame that alter expression. These act by binding to transcription factors which then cause the DNA to loop so that the regulatory sequence (and bound transcription factor) become close to the RNA polymerase binding site. For example, enhancers increase transcription by binding an activator protein which then helps to recruit the RNA polymerase to the promoter; conversely silencers bind repressor proteins and make the DNA less available for RNA polymerase. The transcribed pre-mRNA contains untranslated regions at both ends which contain a ribosome binding site, terminator and start and stop codons. In addition, most eukaryotic open

neg: Ribosome RNA and associated proteins that function to synthesize proteins. Proteins are needed for many cellular functions such as repairing damage or directing chemical processes. Ribosomes can be found floating within the cytoplasm or attached to the endoplasmic reticulum. Ribosomes act as catalysts in two extremely important biological processes called peptidyl transfer and peptidyl hydrolysis. The "PT center is responsible for producing protein bonds during protein elongation". Ribosomes are the workplaces of protein biosynthesis, the process of translating mRNA into protein. The mRNA comprises a series of codons that dictate to the ribosome the sequence of the amino acids needed to

neg: RNA polymerase II holoenzyme of the cap-synthesizing and cap-binding complex. In eukaryotes, after transcription of the 5' end of an RNA transcript, the cap-synthesizing complex on the CTD will remove the gamma-phosphate from the 5'-phosphate and attach a GMP, forming a 5',5'-triphosphate linkage. The synthesizing complex falls off and the cap then binds to the cap-binding complex (CBC), which is bound to the CTD. The 5'cap of eukaryotic RNA transcripts is important for binding of the mRNA transcript to the ribosome during translation, to the CTD of RNAP, and prevents RNA degradation. The carboxy-terminal domain is also the binding site for spliceosome factors that

neg: Measles Measles virus uses a protein on its surface called hemagglutinin (H protein), to bind to a target receptor on the host cell, which could be CD46, which is expressed on all nucleated human cells, CD150, aka signaling lymphocyte activation molecule or SLAM, which is found on immune cells like B or T cells, and antigen-presenting cells, or nectin-4, a cellular adhesion molecule. Once bound, the fusion, or F protein helps the virus fuse with the membrane and ultimately get inside the cell. The virus is a single-stranded negative-sense RNA virus meaning it first has to be transcribed by RNA polymerase

neg: RNA interference for binding of RNA to the argonaute protein was examined by X-ray crystallography of the binding domain of an RNA-bound argonaute protein. Here, the phosphorylated 5' end of the RNA strand enters a conserved basic surface pocket and makes contacts through a divalent cation (an atom with two positive charges) such as magnesium and by aromatic stacking (a process that allows more than one atom to share an electron by passing it back and forth) between the 5' nucleotide in the siRNA and a conserved tyrosine residue. This site is thought to form a nucleation site for the binding of

neg: Silencer (genetics) bind to the operator, which allows RNA polymerase to bind to the promoter to initiate transcription of the operon. When the repressor's allosteric site is not bound to lactose, its active site will bind to the operator to prevent RNA polymerase from transcribing the genes of the "lac" operon. Eukaryotes have a much larger genome and thus have different methods of gene regulation than in prokaryotes. All cells in a eukaryotic organism have the same DNA but are specified through differential gene expression, a phenomenon known as genetic totipotency. However, in order for a cell to express the genes for

neg: U2 small nuclear RNA auxiliary factor 1 U2 small nuclear RNA auxiliary factor 1 Splicing factor U2AF 35 kDa subunit is a protein that in humans is encoded by the "U2AF1" gene. This gene belongs to the splicing factor SR family of genes. U2 auxiliary factor, comprising a large and a small subunit, is a non-snRNP protein required for the binding of U2 snRNP to the pre-mRNA branch site. This gene encodes the small subunit which plays a critical role in both constitutive and enhancer-dependent RNA splicing by directly mediating interactions between the large subunit and proteins bound to the enhancers. Alternatively spliced transcript variants encoding different

neg: Eukaryotic ribosome (80S) and the body. Characteristic features of the body include the left and right feet, the shoulder and the platform. The head features a pointed protrusion reminiscent of a bird's beak. In the characteristic "crown view" of the large subunit, structural landmarks include the central protuberance, the L1-stalk and the P-stalk. The majority of the eukaryote-specific RNA and protein elements are found on the solvent-exposed sides of the 40S and 60S subunits. The subunit interface, as well as important functional regions such as the peptidyl transferase center and the decoding site are mostly conserved, with some differences observed in the surrounding

neg: Ribosome split apart. Ribosomes are ribozymes, because the catalytic peptidyl transferase activity that links amino acids together is performed by the ribosomal RNA. Ribosomes are often associated with the intracellular membranes that make up the rough endoplasmic reticulum. Ribosomes from bacteria, archaea and eukaryotes in the three-domain system, resemble each other to a remarkable degree, evidence of a common origin. They differ in their size, sequence, structure, and the ratio of protein to RNA. The differences in structure allow some antibiotics to kill bacteria by inhibiting their ribosomes, while leaving human ribosomes unaffected. In bacteria and archaea, more than one ribosome

neg: Prokaryotic DNA replication to DnaA-ATP. During initiation, DnaA bound to high affinity DnaA box R4 donates additional DnaA to the adjacent low affinity site and progressively fill all the low affinity DnaA boxes. Filling of the sites changes origin conformation from its native state. It is hypothesized that DNA stretching by DnaA bound to the origin promotes strand separation which allows more DnaA to bind to the unwound region. The DnaC helicase loader then interacts with the DnaA bound to the single-stranded DNA to recruit the DnaB helicase, which will continue to unwind the DNA as the DnaG primase lays down an RNA

neg: Cas9 RNA (sgRNA, in red) which has been proved to have the same function as the natural RNA complex. The sgRNA base paired with target ssDNA is anchored by Cas9 as a T-shaped architecture. This crystal structure of the DNA-bound Cas9 enzyme reveals distinct conformational changes in the alpha-helical lobe with respect to the nuclease lobe, as well as the location of the HNH domain. The protein consists of a recognition lobe (REC) and a nuclease lobe (NUC). It should be noted that all regions except the HNH form tight interactions with each other and sgRNA-ssDNA complex, while the HNH domain

neg: Eukaryotic ribosome (80S) mutations of the linker between the core of rpS27A(S31) and the ubiquitin domain are lethal in yeast. Comparisons between bacterial, archaeal and eukaryotic ribosome structures reveal a very high degree of conservation in the active site—aka the peptidyl transferase center (PTC) -- region. None of the eukaryote-specific protein elements is close enough to directly participate in catalysis. However, RPL29 projects to within 18Å of the active site in "T. thermophila", and eukaryote-specific extensions interlink several proteins in the vicinity of the PTC of the 60S subunit, while the corresponding 50S proteins are singular entities. Contacts across the two ribosomal subunits

neg: GC-content G (guanine) and C (cytosine) undergo a specific hydrogen bonding, whereas A (adenine) bonds specifically with T (thymine, in DNA) or U (uracil, in RNA). Quantitativelty, the GC pair is bound by three hydrogen bonds, while AT and AU pairs are bound by two hydrogen bonds. To emphasize this difference in the number of hydrogen bonds, the base pairings can be represented as respectively G≡C versus A=T and A=U. DNA with low GC-content is less stable than DNA with high GC-content; however, the hydrogen bonds themselves do not have a particularly significant impact on stabilization, the stabilization is due mainly

neg: Epitranscriptomic sequencing on full-length RNA using m6A-specific antibody [36]. UV light at 365 nm is then shined onto RNA to activate the crosslinking to the antibody with 4SU. Crosslinked RNA was isolated via competition elution and fragmented further to ~25-30nt; proteinase K was used to dissociate the covalent bond between crosslinking site and antibody. Peptide fragments that remain after antibody removal from RNA cause the base to be read as a C as opposed to a T during reverse transcription, effectively inducing a point mutation at the 4SU crosslinking site. The short fragments are subjected to library construction and Illumina sequencing, followed

neg: Diagnosis of HIV/AIDS opened to release its RNA. Special oligonucleotides that bind to viral RNA and to certain oligonucleotides bound to the wall of the vessel are added. In this way, viral RNA is fastened to the wall. Then new oligonucleotides that bind at several locations to this RNA are added, and other oligonucelotides that bind at several locations to those oligonucleotides. This is done to amplify the signal. Finally, oligonucleotides that bind to the last set of oligonucleotides and that are bound to an enzyme are added; the enzyme action causes a color reaction, which allows quantification of the viral RNA in

neg: Twister sister ribozyme pre-catalytic state of the twister sister ribozymes were solved by two research groups independently. The structure of a three-way junctional twister sister ribozyme is composed of two co-axial stacked helical sections connected with a three-way junction and two tertiary contacts. The active site, a scissile phosphate, is located in a loop with quasihelical character in one coaxial base-stacked helix. Five divalent metal ions are coordinate to RNA ligands, one of which is directly bound to C O2’ near the scissile phosphate and exchange inner sphere water molecules with the RNA ligands. The crystal structure of a four-way junctional twister sister

neg: C1QL1 with the T/A site detected just once. Both sites are found within exon 1. Q/R site This site is found in exon 1 at position 66. Editing results in a codon change from a Glutamine codon to an Arginine codon. T/A site This site is also found in exon 1, at position 63. It was only detected in one genomic sample indicating that the edited residue may be an SNP. However, the secondary structure of the RNA is predicted, around the editing site, to be highly conserved in mice and humans. This indicates that the T/A site may still be

neg: Lac operon organized into an operon; that is, they are oriented in the same direction immediately adjacent on the chromosome and are co-transcribed into a single polycistronic mRNA molecule. Transcription of all genes starts with the binding of the enzyme RNA polymerase (RNAP), a DNA-binding protein, which binds to a specific DNA binding site, the promoter, immediately upstream of the genes. Binding of RNA polymerase to the promoter is aided by the cAMP-bound catabolite activator protein (CAP, also known as the cAMP receptor protein). However, the "lacI" gene (regulatory gene for "lac" operon) produces a protein that blocks RNAP from binding to

neg: RNA spike-in DNA microarrays are solid surfaces, usually a small chip, to which short DNA polymers of known sequence are covalently bound. When a sample of unknown RNA is flowed over the array, the RNA base pairs with and binds to complementary DNA. Bound transcripts can be detected, indicating the presence of RNA with the corresponding sequence. DNA microarray assays are useful in studies of gene expression, because many of the mRNA transcripts present in a cell can be detected at the same time. RNA spike-ins of known quantity can provide a baseline signal for comparison with the signal from transcripts of

neg: Ribosome are made of 50S and 30S subunits. Prokaryotes have 70S ribosomes, each consisting of a small (30S) and a large (50S) subunit. Their small subunit has a 16S RNA subunit (consisting of 1540 nucleotides) bound to 21 proteins. The large subunit is composed of a 5S RNA subunit (120 nucleotides), a 23S RNA subunit (2900 nucleotides) and 31 proteins. Affinity label for the tRNA binding sites on the E. coli ribosome allowed the identification of A and P site proteins most likely associated with the peptidyltransferase activity; labelled proteins are L27, L14, L15, L16, L2; at least L27 is located

neg: Bacterial DNA binding protein promoter decreasing rRNA production during stationary and slow growth periods. RNA polymerase and H-NS DNA binding protein have overlapping binding sites; it is thought that H-NS regulates rRNA production by acting on the transcription initiation site. It has been found that H-NS and RNA polymerase both bind to the P1 promoter and form a complex. When H-NS is bound with RNA Polymerase to the promoter region, there are structural differences in the DNA that are accessible. It has also been found that H-NS can affect translation as well by binding to mRNA and causing its degradation. HU is a small

neg: Var1 protein domain aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites. Since Var1 helps form the small subunit of the ribosome, its significance become apparent in translation and cell survival. Var1 protein domain In molecular biology, VAR1 protein domain, otherwise known as variant protein 1, is a

neg: Prokaryotic translation the A site, the P site, and the E site. The "A site" is the point of entry for the aminoacyl tRNA (except for the first aminoacyl tRNA, which enters at the P site). The "P site" is where the peptidyl tRNA is formed in the ribosome. And the "E site" which is the exit site of the now uncharged tRNA after it gives its amino acid to the growing peptide chain. The selection of an initiation site (usually an AUG codon) depends on the interaction between the 30S subunit and the mRNA template. The 30S subunit binds to the

neg: Small nucleolar RNA SNORD50 box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. U50 is an intronic snoRNA gene located on chromosome 6q15, at the breakpoint of chromosomal translocation t(3;6)(q27;q15). The U50HG gene is composed of six exons, whose spliced transcripts have little potential for coding a protein, and its introns produce both U50 and U50-like (U50') snoRNAs that are localised in nucleoli. There is evidence that the U50 paralogues form a novel family of genes controlling oncogenesis and sensitivity to therapy in cancer. Small nucleolar RNA SNORD50 snoRNA U50 (also known as SNORD50) is a non-coding RNA (ncRNA) molecule which functions

neg: Daptomycin release, of the free C-10 fatty acid. To synthesize the peptide portion of daptomycin, the mechanism of an NRPS is employed. The biosynthetic machinery of an NRPS system is composed of multimodular enzymatic assembly lines that contain one module for each amino acid monomer incorporated. Within each module are catalytic domains that carry out the elongation of the growing peptidyl chain. The growing peptide is covalently tethered to a thiolation domain; here it is termed the peptidyl carrier protein, as it carries the growing peptide from one catalytic domain to the next. Again, the apo-T domain must be primed to

neg: Prokaryotic large ribosomal subunit divided into six large domains, within which domain V is most important in its peptidyl transferase activity. Each domain contains normal secondary structure (e.g., base triple, tetraloop, cross-strand purine stack) and is also highly symmetric in tertiary structure; proteins intervene between their helices. At tertiary structure level, the large subunit rRNA is a single gigantic domain while the small subunit contains three structural domains. This difference reflects the lesser flexibility of the large subunit required by its function. 50S includes the activity that catalyzes peptide bond formation (peptidyl transfer reaction), prevents premature polypeptide hydrolysis, provides a binding site for the

neg: Feline morbillivirus macrophages, B- and T-cells. This offers clear information as to why "morbilliviruses" can very quickly infect immune cells. Another newly discovered cellular receptor called PVRL4 allows for "morbillivirus" entry into bronchial epithelial cells and keratinocytes. Additionally, the "Feline morbillivirus" F protein is known to have a single cleavage site that splits the protein into separate F1 and F2 proteins which play an important role in fusing the viral and cellular membranes together during entry. Since this virus possesses a negative-sense RNA genome, its replication and transcription cycles follow that of the negative-RNA genome. Therefore, to replicate, the negative, single-stranded RNA

neg: RNA-targeting small molecule drugs chemistry to screen a compound library against HIV-1 frameshift regulatory stem-loop RNA. They identified a hit compound that was selective for the regulatory sequence with micromolar binding affinity. In 2011, Butcher and colleagues discovered a frameshifting stimulator (DB213) which bound to HIV-1 FS RNA with moderate binding affinity. An NMR structure of the RNA in complex with DB213, showed that the small molecule bound to the major groove of the RNA duplex. Schneekloth and Hargrove have taken a different approach by targeting the HIV-1 TAR RNA hairpin. In a small molecule microarray screening, the Schneekloth group identified a thienopyridine derivative

neg: Leroy Hood This research led to verification of the "two genes, one polypeptide" hypothesis and insights into the mechanisms responsible for the diversification of the immunoglobulin variable genes. Hood shared the Lasker Award in 1987 for these studies. Additionally, Hood was among the first to study, at the gene level, the MHC (major histocompatibility complex) gene family and the T-cell receptor gene families as well as being among first to demonstrate that alternative RNA splicing was a fundamental mechanism for generating alternative forms of antibodies. He showed that RNA splicing is the mechanism for generating the membrane bound and the secreted forms

neg: Lincosamides the synthesis of proteins. In a mechanism similar to macrolides and streptogramin B, lincosamides bind close to the peptidyl transferase center on the 23S portion of the 50S subunit of bacterial ribosomes. High resolution X-ray structures of clindamycin and ribosomal subunits from bacterium have previously revealed exclusive binding to the 23s segment of the peptidyl transferase cavity. Binding is mediated by the mycarose sugar moiety which has partially overlapping substrates with peptidyl transferase. By extending to the peptidyl transferase center, lincosamides cause the premature dissociation of peptidyl-tRNA's containing two, three or four amino acid residues. In this case, peptides will

neg: VA RNA shown that VAI-RNA increases the stability of ribosome-bound transcripts. VAI RNA is processed in the cell to create 22 nucleotide long RNAs that can act as siRNA or miRNA. VAI RNA functions as a decoy RNA for the double stranded RNA activated protein kinase R which would otherwise phosphorylate eukaryotic initiation factor 2. VA RNA is composed of two stem-loops separated by a central region essential for function. VA RNA The VA (viral associated) RNA is a type of non-coding RNA found in adenovirus. It plays a role in regulating translation. There are two copies of this RNA called VAI

neg: Bottromycin made bottromycin a more target for drug development, especially given the rise of antibiotic resistance. The mechanism of action of bottromycin was confirmed nearly 20 years following the discovery of bottromycin. Bottromycin functions as an antibiotic through inhibition of protein synthesis. It blocks aminoacyl "t"RNA binding to the ribosome by binding to the A site of the 50s subunit. This results in release of aminoacyl "t"RNA from the ribosome and premature termination of protein synthesis. A comparison of other antiobiotics known to bind to the A site of the ribosome, including micrococcin, tetracycline, streptomycin, and chloramphenicol, suggested that only bottromycin

neg: Regulator gene or negative regulators, based on the environmental conditions that surround the cell. Positive regulators are regulatory elements that permit RNA polymerase binding to the promoter region, thus allowing transcription to occur. In terms of the lac operon, the positive regulator would be the CRP-cAMP complex that must be bound close to the site of the start of transcription of the lac genes. The binding of this positive regulator allows RNA polymerase to bind successfully to the promoter of the lac gene sequence which advances the transcription of lac genes; lac Z, lac Y, and lac A. Negative regulators are regulatory

neg: Bwamba Fever into three pieces, Large (L), Medium (M) and Small (S), which have a combined length of approximately 12,000nt. The S RNA encodes a nucleocapsid and non structural proteins, the M RNA encodes envelope glycoproteins and a non structural membrane polypeptide and the L RNA encodes an RNA dependent RNA polymerase. The segmented RNAs are surrounded by nucleocapsid proteins that form a Ribonucleoprotein complex, that associates with RNA dependent RNA polymerase. The complex is surrounded by a lipid layer, into which the nuclear complex interacts. Finally the particle is membrane bound, spherical, and in total is approximately 100 nm in diameter.

neg: OxyS RNA OxyS RNA OxyS RNA is a small non-coding RNA which is induced in response to oxidative stress in "Escherichia coli". This RNA acts as a global regulator to activate or repress the expression of as many as 40 genes, by an antisense mechanism, including the fhlA-encoded transcriptional activator and the rpoS-encoded sigma(s) subunit of RNA polymerase. OxyS is bound by the Hfq protein, that increases the OxyS RNA interaction with its target messages. Binding to Hfq alters the conformation of OxyS. The 109 nucleotide RNA is thought to be composed of three stem-loops. A number of additional targets were predicted

neg: 5S ribosomal RNA and other proteins of the central protuberance of the LSU plays a role in binding tRNAs. Also, the topographical and physical proximity between 5S rRNA and 23S rRNA, which forms the peptidyl transferase and GTPase-associating center, suggests that 5S rRNA acts as a mediator between the two functional centers of the ribosome by forming, together with 5S rRNA-binding proteins and other components of the central protuberance, intersubunit bridges and tRNA-binding sites. In eukaryotes, the cytosolic ribosome is assembled from four rRNAs and over 80 proteins. Once transcribed, the 3' ends of 5S rRNA are processed by the exonucleases Rex1p, Rex2p,

neg: Cpf1 in human cells. Cpf1 was introduced with features that SpCas9 is lacking. Cpf1 requires only a 42-nt short CRISPR RNA (crRNA) to find its target, instead of the ~100-nt guide RNA for SpCas9, and it recognizes a protospacer-adjacent motif (PAM) that is 5′ instead of 3′ of the target site. Cpf1 In molecular biology, CRISPR-associated endonuclease in Prevotella and Francisella 1 or Cpf1 is a single RNA-guided endonuclease lacking a small trans-encoded RNA, a tracrRNA, and it utilizes a T-rich protospacer-adjacent motif of 2-6 base pair DNA sequence immediately following the DNA sequence targeted by the Cas9 nuclease in the

neg: Biosynthesis an anticodon that base pairs with specific nucleotide triplets on the mRNA called codons; codons encode a specific amino acid. This interaction is possible thanks to the ribosome, which serves as the site for protein synthesis. The ribosome possesses three tRNA binding sites: the aminoacyl site (A site), the peptidyl site (P site), and the exit site (E site). There are numerous codons within an mRNA transcript, and it is very common for an amino acid to be specified by more than one codon; this phenomenon is called degeneracy. In all, there are 64 codons, 61 of each code for

neg: Lincosamides grow to a certain point until steric hindrance inhibits peptidyl transferase activity. Lincosamides do not interfere with protein synthesis in human cells (or those of other eukaryotes) due to structural differences between prokaryotic and eukaryotic ribosomes. Lincosamides are used against Gram positive bacteria since they are unable to pass through the porins of Gram-negative bacteria. Soon after the emergence of clinical lincosamide use in 1953, strains of resistant staphylococci were isolated in several countries including France, Japan and the United States. Resistant strains were characterized by expression of methyltransferases which demethylate residues within the 23S subunit of ribosomal RNA, preventing

neg: Linezolid synthesis inhibitor and a weak, non-selective, reversible monoamine oxidase inhibitor. As a protein synthesis inhibitor, linezolid stops the growth and reproduction of bacteria by disrupting translation of messenger RNA (mRNA) into proteins in bacterial ribosomes. Linezolid inhibits translation at the first step of protein synthesis, "initiation", unlike most other protein synthesis inhibitors, which inhibit "elongation". It does so by preventing the formation of the initiation complex, composed of the 30S and 50S subunits of the ribosome, tRNA, and mRNA. Linezolid binds to the 23S portion of the 50S subunit (the center of peptidyl transferase activity), close to the binding sites

neg: ChiRP-Seq + RNA of interest + DNA fragment are captured by magnetic beads labeled with streptavidin. DNA is isolated from an aliquot of the bound complex by treatment with RNAse (or proteinase followed by RNAse) to digest associated protein and RNA. RNA may also be isolated from an additional aliquot of the bound complex to detect other RNA molecules associated with the RNA of interest. The purified DNA is then used to prepare a sequencing library and the library is sequenced on a next generation DNA sequencing system. The sequencing reads are then mapped to the genome. A pile-up of reads

neg: OxyS RNA and verified using microarray analysis. These are listed below: Furthermore, the mRNA encoded by the "nusG" gene is a direct target of OxyS. OxyS RNA OxyS RNA is a small non-coding RNA which is induced in response to oxidative stress in "Escherichia coli". This RNA acts as a global regulator to activate or repress the expression of as many as 40 genes, by an antisense mechanism, including the fhlA-encoded transcriptional activator and the rpoS-encoded sigma(s) subunit of RNA polymerase. OxyS is bound by the Hfq protein, that increases the OxyS RNA interaction with its target messages. Binding to Hfq alters

neg: Messenger RNP Messenger RNP Messenger RNP (messenger ribonucleoprotein) is mRNA with bound proteins. mRNA does not exist "naked" "in vivo" but is always bound by various proteins while being synthesized, spliced, exported, and translated in the cytoplasm. When mRNA is being synthesized by RNA polymerase, this nascent mRNA is already bound by RNA 5′ end 7-methyl-guanosine capping enzymes. Later, the pre-mRNA is bound by the spliceosome containing exon and intron definition complexes and proteins and RNA that catalyze the chemical reactions of splicing. Joan Steitz and Michael Lerner and collaborators showed that the small nuclear RNAs (snRNAs) are complexed into small nuclear

neg: Signal recognition particle signal peptidase. Signal sequences are therefore not a part of mature proteins. Despite SRP function being analogous in all organisms, its composition varies greatly. The eukaryotic SRP is composed of six distinct polypeptides bound to an RNA molecule (the 7SL RNA), with GTPase activity. The components of the complex are: The prokaryotic SRP is composed of one polypeptide bound to an RNA molecule (the 4.5S RNA), with GTPase activity. The components of the complex are: Ffh is the structural and functional homolog of the SRP54 protein in eukaryotes. The 4.5S RNA shares sequence and structural homology with one domain of

neg: Eukaryotic transcription Once the initiation complex is open, the first ribonucleotide is brought into the active site to initiate the polymerization reaction in the absence of a primer. This generates a nascent RNA chain that forms a hetero-duplex with the template DNA strand. However, before entering the elongation phase, polymerase may terminate prematurely and release a short, truncated transcript. This process is called abortive initiation. Many cycles of abortive initiation may occur before the transcript grows to sufficient length to promote polymerase escape from the promoter. Throughout abortive initiation cycles, RNA polymerase remains bound to the promoter and pulls downstream DNA into

neg: Daptomycin the holo-T domain by a PPTase, attaching a flexible phosphopantetheine arm to a conserved serine residue. An adenylation domain selects the amino acid monomer to be incorporated and activates the carboxylate with ATP to make the aminoacyl-AMP. Next, the A domain installs an aminoacyl group on the thiolate of the adjacent T domain. The condensation (C) domain catalyzes the peptide bond forming reaction, which elicits chain elongation. It joins an upstream peptidyl-S-T to the downstream aminoacyl-S-T (Figure 7). Chain elongation by one aminoacyl residue and chain translocation to the next T domain occurs in concert. The order of these domains

neg: Prp8 at the 5’ end of the mRNA before shifting to introns. The U5 snRNP is involved with Complex C, the catalytic spliceosome, where the U5 snRNP binds to an exon at the 3’ splice site and the lariat loop forms. The U5 snRNP is also involved with Complex C*, the post-catalytic spliceosome, where it remains bound to the lariat before the spliced RNA is released and the snRNPs are recycled. Common research methods for studying the structure and functions of Prp8 are co-immunoprecipitation and Western blot analysis. The structure of Prp8 includes a RNA recognition motif, a MPN / JAB

neg: Bacterial transcription proteins called transcription factors. The following steps occur, in order, for transcription initiation:. "promoter", and |T| stands for the "terminator". The DNA on the template strand between the +1 site and the terminator is transcribed into RNA, which is then translated into protein. At this stage, the DNA is double-stranded ("closed"). This holoenzyme/wound-DNA structure is referred to as the "closed complex". Promoters can differ in "strength"; that is, how actively they promote transcription of their adjacent DNA sequence. Promoter strength is in many (but not all) cases, a matter of how tightly RNA polymerase and its associated accessory proteins bind

neg: Somatic hypermutation A are observed to exceed mutations of T (A»>T) and mutations of G are observed to exceed mutations of C (G»>C). This involves error-prone cDNA synthesis via an RNA-dependent DNA polymerase copying the base modified Ig pre-mRNA template and integrating the now error-filled cDNA copy back into the normal chromosomal site. The errors in the Ig pre-mRNA are a combination of adenosine-to-inosine (A-to-I) RNA editing and RNA polymerase II transcription elongation complex copying uracil and abasic sites (arising as AID-mediated lesions) into the nascent pre-mRNA using the transcribed (TS) DNA as the copying template strand. The modern form of this

neg: Small nucleolar RNA U2-30 C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. snoRNA U2-30 directs 2'-O-methylation of U2 spliceosomal RNA A-30. Small nucleolar RNA U2-30 Small nucleolar RNA U2-30 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA U2-30 belongs to the C/D box class of snoRNAs which contain the conserved sequence

neg: Small nucleolar RNA U2-19 C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. snoRNA U2-19 directs 2'-O-methylation of U2 spliceosomal RNA G-19. Small nucleolar RNA U2-19 Small nucleolar RNA U2-19 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA U2-19 belongs to the C/D box class of snoRNAs which contain the conserved sequence

neg: Eukaryotic release factors protein release factors (RFs) and GTP. A class 1 RF recognizes the stop codon and promotes the hydrolysis of the ester bond linking the polypeptide chain with the peptidyl site tRNA, a reaction catalyzed at the peptidyl transferase center of the ribosome. Class 2 RFs, which are not codon specific and do not recognize codons, stimulate class 1 RF activity and confer GTP dependency upon the process. In prokaryotes, both class 1 RFs, RF1 and RF2, recognize UAA; however, UAG and UGA are decoded specifically by RF1 and RF2, respectively. In eukaryotes, eRF1, or ETF1, the functional counterpart of RF1

neg: Telomerase of telomerase are dependent on an intact RNA template. Cancer stem cells that use an alternative method of telomere maintenance are still killed when telomerase's RNA template is blocked or damaged. Two telomerase vaccines have been developed: GRNVAC1 and GV1001. GRNVAC1 isolates dendritic cells and the RNA that codes for the telomerase protein and puts them back into the patient to make cytotoxic T cells that kill the telomerase-active cells. GV1001 is a peptide from the active site of hTERT and is recognized by the immune system that reacts by killing the telomerase-active cells. Another independent approach is to use

neg: Small nucleolar RNA SNORD23 directing site-specific 2'-O-methylation of substrate RNAs. This snoRNA is the human orthologue of mouse snoRNA MBII-115. There is currently no predicted target RNA for SNORD23. Small nucleolar RNA SNORD23 Small Nucleolar RNA SNORD23 (also known as HBII-115) is a non-coding RNA (ncRNA) molecule which functions in the biogenesis (modification) of other small nuclear RNAs (snRNAs). This type of modifying RNA is located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. SNORD23 belongs to the C/D

neg: Small nucleolar RNA SNORD98 directing site-specific 2'-O-methylation of substrate RNAs. SNORD98 is predicted to guide the 2'0-ribose methylation of 18S ribosomal RNA (rRNA) residue G867. Small nucleolar RNA SNORD98 Small Nucleolar RNA SNORD98 (also known as HBII-419) is a non-coding RNA (ncRNA) molecule which functions in the biogenesis (modification) of other small nuclear RNAs (snRNAs). This type of modifying RNA is located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. SNORD98 belongs to the C/D box class of snoRNAs

neg: Small nucleolar RNA base complementary to the sequence surrounding the base (nucleotide) targeted for modification in the pre-RNA molecule. This enables the snoRNP to recognise and bind to the target RNA. Once the snoRNP has bound to the target site, the associated proteins are in the correct physical location to catalyse the chemical modification of the target base. The two different types of rRNA modification (methylation and pseudouridylation) are directed by two different families of snoRNAs. These families of snoRNAs are referred to as antisense C/D box and H/ACA box snoRNAs based on the presence of conserved sequence motifs in the snoRNA. There

neg: Thomas A. Steitz Thomas A. Steitz Thomas Arthur Steitz (August 23, 1940 – October 9, 2018) was an American biochemist, a Sterling Professor of Molecular Biophysics and Biochemistry at Yale University, and investigator at the Howard Hughes Medical Institute, best known for his pioneering work on the ribosome. Steitz was awarded the 2009 Nobel Prize in Chemistry along with Venkatraman Ramakrishnan and Ada Yonath "for studies of the structure and function of the ribosome". Steitz also won the Gairdner International Award in 2007 "for his studies on the structure and function of the ribosome which showed that the peptidyl transferase was an RNA

neg: Small nucleolar RNA Z155 C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. Plant snoRNA Z155 was identified in a screen of "Oryza sativa". Small nucleolar RNA Z155 Small nucleolar RNA Z155 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA Z155 belongs to the C/D box class of snoRNAs which contain the

neg: Small nucleolar RNA Z119 C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. Plant snoRNA Z119 was identified in a screen of "Oryza sativa". Small nucleolar RNA Z119 Small nucleolar RNA Z119 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA Z119 belongs to the C/D box class of snoRNAs which contain the

neg: Small nucleolar RNA Z112 C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. Plant snoRNA Z112 was identified in a screen of "Oryza sativa". Small nucleolar RNA Z112 Small nucleolar RNA Z112 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA Z112 belongs to the C/D box class of snoRNAs which contain the

neg: Small nucleolar RNA Z103 C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. Plant snoRNA Z103 was identified in a screen of "Oryza sativa". Small nucleolar RNA Z103 Small nucleolar RNA Z103 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA Z103 belongs to the C/D box class of snoRNAs which contain the

neg: Small nucleolar RNA Z101 C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. Plant snoRNA Z101 was identified in a screen of "Oryza sativa". Small nucleolar RNA Z101 Small nucleolar RNA Z101 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA Z101 belongs to the C/D box class of snoRNAs which contain the

neg: Small nucleolar RNA snoR60 C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. Plant snoRNA snoR60 was identified in a screen of "Arabidopsis thaliana". Small nucleolar RNA snoR60 Small nucleolar RNA snoR60 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA snoR60 belongs to the C/D box class of snoRNAs which contain the

neg: Small nucleolar RNA snoR28 C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. Plant snoRNA R28 was identified in a screen of "Arabidopsis thaliana". Small nucleolar RNA snoR28 Small nucleolar RNA R28 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA R28 belongs to the C/D box class of snoRNAs which contain the

neg: Small nucleolar RNA snoR1 C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. Plant snoRNA snoR1 was identified in a screen of "Arabidopsis thaliana". Small nucleolar RNA snoR1 Small nucleolar RNA snoR1 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA snoR1 belongs to the C/D box class of snoRNAs which contain the

neg: Small nucleolar RNA R79 C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. Plant snoRNA R79 was identified in a screen of "Arabidopsis thaliana". Small nucleolar RNA R79 Small nucleolar RNA R79 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA R79 belongs to the C/D box class of snoRNAs which contain the

neg: Small nucleolar RNA R43 C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. Plant snoRNA R43 was identified in a screen of "Arabidopsis thaliana". Small nucleolar RNA R43 Small nucleolar RNA R43 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA R43 belongs to the C/D box class of snoRNAs which contain the

neg: Small nucleolar RNA R21 C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. Plant snoRNA R21 was identified in a screen of "Arabidopsis thaliana" Small nucleolar RNA R21 Small nucleolar RNA R21 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA R21 belongs to the C/D box class of snoRNAs which contain the

neg: Small nucleolar RNA R20 C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. Plant snoRNA R20 was identified in a screen of "Arabidopsis thaliana". Small nucleolar RNA R20 Small nucleolar RNA R20 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA R20 belongs to the C/D box class of snoRNAs which contain the

neg: Small nucleolar RNA J33 C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. Plant snoRNA J33 was identified in a screen of "Oryza sativa". Small nucleolar RNA J33 Small nucleolar RNA J33 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA J33 belongs to the C/D box class of snoRNAs which contain the

neg: Small nucleolar RNA J26 members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. Small nucleolar RNA J26 Small nucleolar RNA J26 is a non-coding RNA (ncRNA) molecule identified in rice ("Oryza sativa") which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. J26 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs

neg: Z6 small nucleolar RNA C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. Z6 small nucleolar RNA Z6 small nucleolar RNA is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. Z6 snoRNA belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the