Exoribonucleases
Polyribonucleotide Nucleotidyltransferase
RNA, Transfer, Tyr
Exosome Multienzyme Ribonuclease Complex
Endoribonucleases
RNA, Ribosomal, 5.8S
RNA Processing, Post-Transcriptional
RNA Stability
RNA, Bacterial
RNA Precursors
Ribonuclease III
Escherichia coli
RNA
Molecular Sequence Data
RNA, Messenger
NMD3 encodes an essential cytoplasmic protein required for stable 60S ribosomal subunits in Saccharomyces cerevisiae. (1/762)
A mutation in NMD3 was found to be lethal in the absence of XRN1, which encodes the major cytoplasmic exoribonuclease responsible for mRNA turnover. Molecular genetic analysis of NMD3 revealed that it is an essential gene required for stable 60S ribosomal subunits. Cells bearing a temperature-sensitive allele of NMD3 had decreased levels of 60S subunits at the nonpermissive temperature which resulted in the formation of half-mer polysomes. Pulse-chase analysis of rRNA biogenesis indicated that 25S rRNA was made and processed with kinetics similar to wild-type kinetics. However, the mature RNA was rapidly degraded, with a half-life of 4 min. Nmd3p fractionated as a cytoplasmic protein and sedimented in the position of free 60S subunits in sucrose gradients. These results suggest that Nmd3p is a cytoplasmic factor required for a late cytoplasmic assembly step of the 60S subunit but is not a ribosomal protein. Putative orthologs of Nmd3p exist in Drosophila, in nematodes, and in archaebacteria but not in eubacteria. The Nmd3 protein sequence does not contain readily recognizable motifs of known function. However, these proteins all have an amino-terminal domain containing four repeats of Cx2C, reminiscent of zinc-binding proteins, implicated in nucleic acid binding or protein oligomerization. (+info)Identification of RNase T as a high-copy suppressor of the UV sensitivity associated with single-strand DNA exonuclease deficiency in Escherichia coli. (2/762)
There are three known single-strand DNA-specific exonucleases in Escherichia coli: RecJ, exonuclease I (ExoI), and exonuclease VII (ExoVII). E. coli that are deficient in all three exonucleases are abnormally sensitive to UV irradiation, most likely because of their inability to repair lesions that block replication. We have performed an iterative screen to uncover genes capable of ameliorating the UV repair defect of xonA (ExoI-) xseA (ExoVII-) recJ triple mutants. In this screen, exonuclease-deficient cells were transformed with a high-copy E. coli genomic library and then irradiated; plasmids harvested from surviving cells were used to seed subsequent rounds of transformation and selection. After several rounds of selection, multiple plasmids containing the rnt gene, which encodes RNase T, were found. An rnt plasmid increased the UV resistance of a xonA xseA recJ mutant and uvrA and uvrC mutants; however, it did not alter the survival of xseA recJ or recA mutants. RNase T also has amino acid sequence similarity to other 3' DNA exonucleases, including ExoI. These results suggest that RNase T may possess a 3' DNase activity capable of substituting for ExoI in the recombinational repair of UV-induced lesions. (+info)Oligoribonuclease is an essential component of the mRNA decay pathway. (3/762)
mRNA decay in prokaryotic cells involves the action of both endo- and exoribonucleases. In Escherichia coli, degradation of RNA to the mononucleotide level was thought to depend on RNase II and polynucleotide phosphorylase. Here, we show that the enzyme oligoribonuclease is an essential part of this process as well. Thus, inactivation of the orn gene encoding oligoribonuclease leads to a cessation of cell growth. Moreover, although pulse-labeled RNA decays normally in orn mutant cells under nonpermissive conditions, a large fraction of the resulting products is small oligoribonucleotides rather than the mononucleotides generated in wild-type cells. The oligoribonucleotides that accumulate are 2-5 residues in length; longer molecules disappear during the decay process. These data indicate that oligoribonuclease is required to complete the degradation of mRNA to mononucleotides and that this process is required for cell viability. Inasmuch as close homologues of the orn gene are found in a wide range of eukaryotes, extending up to humans, these findings raise the possibility that oligoribonuclease also participates in mRNA degradation in these organisms. (+info)Endogenous apurinic/apyrimidinic sites in genomic DNA of mammalian tissues. (4/762)
Apurinic/apyrimidinic (AP) sites are one of the most frequent lesions in DNA. Using a highly sensitive slot blot assay, we determined the number and condition of endogenous AP sites in normal tissues of rats and human liver. The number of AP sites (50,000-200,000 per mammalian cell) was greatest in brain, followed by colon and heart, and then liver, lung, and kidney. The majority of endogenous AP sites were cleaved 5' to the AP site. These data suggest that removal of the deoxyribosyl phosphate moiety is the rate-limiting step in base excision and AP site repair in vivo. (+info)Mutations in translation initiation factors lead to increased rates of deadenylation and decapping of mRNAs in Saccharomyces cerevisiae. (5/762)
The turnover of most mRNAs in Saccharomyces cerevisiae begins with deadenylation followed by decapping and 5'-->3' exonucleolytic digestion. An important question involves the mechanisms that allow particular mRNAs to exhibit different rates of both deadenylation and decapping. Since the cap structure plays a critical role in the assembly of translation initiation factors, we hypothesized that the status of the cytoplasmic cap binding complex would affect the rate of decapping. To test this hypothesis, we examined mRNA decay rates in yeast strains that were defective in several translation initiation factors that are part of the cap binding complex. These experiments yielded three significant observations. First, any mutation known to inhibit translation initiation also increased the rate of decapping. Second, decapping still occurred only after deadenylation, suggesting that the ability of the poly(A) tail to inhibit decapping does not require efficient translation of the transcript. Third, mutants with defects in translation initiation factors also showed an increase in the rate of deadenylation, suggesting that the rate of deadenylation may be controlled primarily by the translation status of the transcript. These results argue that the nature of the translation initiation complex is a critical factor in determining the mRNA half-life. This view also implies that some cis-acting sequences that modulate mRNA decay rate do so by affecting the translation status of the transcript. (+info)tRNAs and proteins are imported into mitochondria of Trypanosoma brucei by two distinct mechanisms. (6/762)
Import of tRNA into the mitochondrial matrix of Trypanosoma brucei was reconstituted in vitro. Efficient import required the hydrolysis of externally added ATP and was shown to be a carrier-mediated process depending on proteinaceous receptors on the surface of mitochondria. A partly synthetic tRNA(Tyr) as well as a physiological tRNA(Lys) were imported along the same pathway. Contrary to import of all matrix-localized proteins, tRNA import does not require a membrane potential. Furthermore, addition of an excess of import-competent tRNA had no effect on import of a mitochondrial matrix protein. In summary, these results show that tRNAs and proteins in T. brucei are imported by fundamentally different mechanisms. (+info)The reaction mechanism of ribonuclease II and its interaction with nucleic acid secondary structures. (7/762)
Ribonuclease II is a processive 3'- to 5'-exoribonuclease in Escherichia coli with two binding sites: a catalytic site associated with the first few 3'-nucleotides and an anchor site binding nucleotides approximately 15 to 25 from the 3'-end. When RNase II degrades single-stranded helical poly(C), the enzyme-substrate complex dissociates at discrete intervals of 12 nucleotides. RNase II stalled at the last rC of single-stranded 3'-(rC)(n)(dC)(m) oligonucleotides. The more residues released, the faster the stalled complex dissociated and the less it inhibited RNase II activity, i.e. the enzyme-substrate association weakened progressively. Using phosphodiesterase I (PDE I) as a probe, a method was developed to identify cytidine residues in (32)P-oligonucleotides interacting with a protein. PAGE bands corresponding to nucleotides 1-6 from the 3'-end were consistent with interaction at the catalytic site, and following a gap, bands approximately 15 to 25 from the 3'-end, with anchor site association. Both 3' and 5' binding were necessary to maintain the complex. Of most significance, the original anchor site nucleotides remained fixed at the anchor site while the 3'-end was pulled, or threaded, through the catalytic site, i.e. the substrate did not 'slide' through the enzyme. DNA oligonucleotides with double-stranded stem-loops were good competitive inhibitors of RNase II. A 3'-single-stranded arm was essential, while optimal binding required both 5'- and 3'-arms. PDE I probing indicated that the nucleotides at the anchor site were specified by the spatial distance from the catalytic site, and on only one of the duplex strands. When degradation of a structured RNA paused or stopped, the RNase II-product commenced cycles of dissociation-reassociation. Duplex strand binding by RNase II made complex DNA or RNA structures accessible to degradation by other nucleases and further verified the PDE I footprinting method. (+info)Active-site mutations in the Xrn1p exoribonuclease of Saccharomyces cerevisiae reveal a specific role in meiosis. (8/762)
Xrn1p of Saccharomyces cerevisiae is a major cytoplasmic RNA turnover exonuclease which is evolutionarily conserved from yeasts to mammals. Deletion of the XRN1 gene causes pleiotropic phenotypes, which have been interpreted as indirect consequences of the RNA turnover defect. By sequence comparisons, we have identified three loosely defined, common 5'-3' exonuclease motifs. The significance of motif II has been confirmed by mutant analysis with Xrn1p. The amino acid changes D206A and D208A abolish singly or in combination the exonuclease activity in vivo. These mutations show separation of function. They cause identical phenotypes to that of xrn1Delta in vegetative cells but do not exhibit the severe meiotic arrest and the spore lethality phenotype typical for the deletion. In addition, xrn1-D208A does not cause the severe reduction in meiotic popout recombination in a double mutant with dmc1 as does xrn1Delta. Biochemical analysis of the DNA binding, exonuclease, and homologous pairing activity of purified mutant enzyme demonstrated the specific loss of exonuclease activity. However, the mutant enzyme is competent to promote in vitro assembly of tubulin into microtubules. These results define a separable and specific function of Xrn1p in meiosis which appears unrelated to its RNA turnover function in vegetative cells. (+info)Exoribonucleases are a type of enzyme that degrade RNA molecules in a process called exoribonucleolysis. They remove nucleotides from the end of an RNA strand, working their way inwards towards the middle of the strand. Exoribonucleases can be specific for single-stranded or double-stranded RNA, and some can discriminate between different types of RNA molecules based on sequence or structure. They play important roles in various cellular processes, including RNA degradation, quality control, and maturation.
Polyribonucleotide nucleotidyltransferase (PRNT) is not a commonly used medical term, but it is a biological term that refers to an enzyme class with the ability to add nucleotides to the 3'-hydroxyl end of RNA molecules. These enzymes play a crucial role in various cellular processes, including RNA metabolism and repair. They can be found in different organisms, from bacteria to humans.
One well-known example of a PRNT is the RNA polymerase, which synthesizes RNA using DNA as a template during transcription. Another example is the telomere-associated polyribonucleotide nucleotidyltransferase, also known as TERT (telomerase reverse transcriptase), which adds repetitive DNA sequences to the ends of chromosomes (telomeres) to maintain their length and stability.
While PRNTs have significant biological importance, they are not typically referred to in a medical context unless discussing specific diseases or conditions related to their dysfunction.
Transfer RNA (tRNA) that specifically carries the amino acid tyrosine (Tyr) during protein synthesis. In genetic code, Tyr is coded by the codons UAC and UAU. The corresponding anticodon on the tRNA molecule is AUA, which pairs with the mRNA codons to bring tyrosine to the ribosome for incorporation into the growing polypeptide chain.
Exosomes are small membrane-bound vesicles that are released by many types of cells into the extracellular space. They contain various proteins, lipids, and nucleic acids, including RNA, which can be taken up by other cells and affect their function.
A multienzyme ribonuclease complex is a group of enzymes that work together to degrade RNA.
Therefore, an "Exosome Multienzyme Ribonuclease Complex" refers to the collection of enzymes found within exosomes that are capable of breaking down RNA. These complexes play a role in regulating the levels of RNA both inside and outside of cells, and may also contribute to intercellular communication by transferring functional RNAs between cells.
Endoribonucleases are enzymes that cleave RNA molecules internally, meaning they cut the phosphodiester bond between nucleotides within the RNA chain. These enzymes play crucial roles in various cellular processes, such as RNA processing, degradation, and quality control. Different endoribonucleases recognize specific sequences or structural features in RNA substrates, allowing them to target particular regions for cleavage. Some well-known examples of endoribonucleases include RNase III, RNase T1, and RNase A, each with distinct substrate preferences and functions.
5.8S ribosomal RNA (rRNA) is a type of structural RNA molecule that is a component of the large subunit of eukaryotic ribosomes. It is one of the several rRNA species that are present in the ribosome, which also include the 18S rRNA in the small subunit and the 28S and 5S rRNAs in the large subunit. The 5.8S rRNA plays a role in the translation process, where it helps in the decoding of messenger RNA (mRNA) during protein synthesis. It is transcribed from DNA as part of a larger precursor RNA molecule, which is then processed to produce the mature 5.8S rRNA. The length of the 5.8S rRNA varies slightly between species, but it is generally around 160 nucleotides long in humans.
Post-transcriptional RNA processing refers to the modifications and regulations that occur on RNA molecules after the transcription of DNA into RNA. This process includes several steps:
1. 5' capping: The addition of a cap structure, usually a methylated guanosine triphosphate (GTP), to the 5' end of the RNA molecule. This helps protect the RNA from degradation and plays a role in its transport, stability, and translation.
2. 3' polyadenylation: The addition of a string of adenosine residues (poly(A) tail) to the 3' end of the RNA molecule. This process is important for mRNA stability, export from the nucleus, and translation initiation.
3. Intron removal and exon ligation: Eukaryotic pre-messenger RNAs (pre-mRNAs) contain intronic sequences that do not code for proteins. These introns are removed by a process called splicing, where the flanking exons are joined together to form a continuous mRNA sequence. Alternative splicing can lead to different mature mRNAs from a single pre-mRNA, increasing transcriptomic and proteomic diversity.
4. RNA editing: Specific nucleotide changes in RNA molecules that alter the coding potential or regulatory functions of RNA. This process is catalyzed by enzymes like ADAR (Adenosine Deaminases Acting on RNA) and APOBEC (Apolipoprotein B mRNA Editing Catalytic Polypeptide-like).
5. Chemical modifications: Various chemical modifications can occur on RNA nucleotides, such as methylation, pseudouridination, and isomerization. These modifications can influence RNA stability, localization, and interaction with proteins or other RNAs.
6. Transport and localization: Mature mRNAs are transported from the nucleus to the cytoplasm for translation. In some cases, specific mRNAs are localized to particular cellular compartments to ensure local protein synthesis.
7. Degradation: RNA molecules have finite lifetimes and undergo degradation by various ribonucleases (RNases). The rate of degradation can be influenced by factors such as RNA structure, modifications, or interactions with proteins.
RNA stability refers to the duration that a ribonucleic acid (RNA) molecule remains intact and functional within a cell before it is degraded or broken down into its component nucleotides. Various factors can influence RNA stability, including:
1. Primary sequence: Certain sequences in the RNA molecule may be more susceptible to degradation by ribonucleases (RNases), enzymes that break down RNA.
2. Secondary structure: The formation of stable secondary structures, such as hairpins or stem-loop structures, can protect RNA from degradation.
3. Presence of RNA-binding proteins: Proteins that bind to RNA can either stabilize or destabilize the RNA molecule, depending on the type and location of the protein-RNA interaction.
4. Chemical modifications: Modifications to the RNA nucleotides, such as methylation, can increase RNA stability by preventing degradation.
5. Subcellular localization: The subcellular location of an RNA molecule can affect its stability, with some locations providing more protection from ribonucleases than others.
6. Cellular conditions: Changes in cellular conditions, such as pH or temperature, can also impact RNA stability.
Understanding RNA stability is important for understanding gene regulation and the function of non-coding RNAs, as well as for developing RNA-based therapeutic strategies.
Bacterial RNA refers to the genetic material present in bacteria that is composed of ribonucleic acid (RNA). Unlike higher organisms, bacteria contain a single circular chromosome made up of DNA, along with smaller circular pieces of DNA called plasmids. These bacterial genetic materials contain the information necessary for the growth and reproduction of the organism.
Bacterial RNA can be divided into three main categories: messenger RNA (mRNA), ribosomal RNA (rRNA), and transfer RNA (tRNA). mRNA carries genetic information copied from DNA, which is then translated into proteins by the rRNA and tRNA molecules. rRNA is a structural component of the ribosome, where protein synthesis occurs, while tRNA acts as an adapter that brings amino acids to the ribosome during protein synthesis.
Bacterial RNA plays a crucial role in various cellular processes, including gene expression, protein synthesis, and regulation of metabolic pathways. Understanding the structure and function of bacterial RNA is essential for developing new antibiotics and other therapeutic strategies to combat bacterial infections.
RNA precursors, also known as primary transcripts or pre-messenger RNAs (pre-mRNAs), refer to the initial RNA molecules that are synthesized during the transcription process in which DNA is copied into RNA. These precursor molecules still contain non-coding sequences and introns, which need to be removed through a process called splicing, before they can become mature and functional RNAs such as messenger RNAs (mRNAs), ribosomal RNAs (rRNAs), or transfer RNAs (tRNAs).
Pre-mRNAs undergo several processing steps, including 5' capping, 3' polyadenylation, and splicing, to generate mature mRNA molecules that can be translated into proteins. The accurate and efficient production of RNA precursors and their subsequent processing are crucial for gene expression and regulation in cells.
Ribonuclease III, also known as RNase III or double-stranded RNA specific endonuclease, is an enzyme that belongs to the endoribonuclease family. This enzyme is responsible for cleaving double-stranded RNA (dsRNA) molecules into smaller fragments of approximately 20-25 base pairs in length. The resulting fragments are called small interfering RNAs (siRNAs), which play a crucial role in the regulation of gene expression through a process known as RNA interference (RNAi).
Ribonuclease III functions by recognizing and binding to specific stem-loop structures within dsRNA molecules, followed by cleaving both strands at precise locations. This enzyme is highly conserved across various species, including bacteria, yeast, plants, and animals, indicating its fundamental role in cellular processes. In addition to its involvement in RNAi, ribonuclease III has been implicated in the maturation of other non-coding RNAs, such as microRNAs (miRNAs) and transfer RNAs (tRNAs).
'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.
While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.
E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.
'Escherichia coli (E. coli) proteins' refer to the various types of proteins that are produced and expressed by the bacterium Escherichia coli. These proteins play a critical role in the growth, development, and survival of the organism. They are involved in various cellular processes such as metabolism, DNA replication, transcription, translation, repair, and regulation.
E. coli is a gram-negative, facultative anaerobe that is commonly found in the intestines of warm-blooded organisms. It is widely used as a model organism in scientific research due to its well-studied genetics, rapid growth, and ability to be easily manipulated in the laboratory. As a result, many E. coli proteins have been identified, characterized, and studied in great detail.
Some examples of E. coli proteins include enzymes involved in carbohydrate metabolism such as lactase, sucrase, and maltose; proteins involved in DNA replication such as the polymerases, single-stranded binding proteins, and helicases; proteins involved in transcription such as RNA polymerase and sigma factors; proteins involved in translation such as ribosomal proteins, tRNAs, and aminoacyl-tRNA synthetases; and regulatory proteins such as global regulators, two-component systems, and transcription factors.
Understanding the structure, function, and regulation of E. coli proteins is essential for understanding the basic biology of this important organism, as well as for developing new strategies for combating bacterial infections and improving industrial processes involving bacteria.
RNA (Ribonucleic Acid) is a single-stranded, linear polymer of ribonucleotides. It is a nucleic acid present in the cells of all living organisms and some viruses. RNAs play crucial roles in various biological processes such as protein synthesis, gene regulation, and cellular signaling. There are several types of RNA including messenger RNA (mRNA), ribosomal RNA (rRNA), transfer RNA (tRNA), small nuclear RNA (snRNA), microRNA (miRNA), and long non-coding RNA (lncRNA). These RNAs differ in their structure, function, and location within the cell.
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.
A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.
Exoribonuclease
Exoribonuclease II
Exoribonuclease H
5'-3' exoribonuclease 2
XRN1 (gene)
Ribonuclease T
POLD1
Exonuclease
Degradosome
RNase D
Ribonuclease E
Exosome complex
Exosome component 2
Terminator (genetics)
RNA editing
DIS3L
P-bodies
Decapping complex
Flavivirus 3' UTR
Oligonucleotidase
Poly(A)-specific ribonuclease
Viral quasispecies
RNase R
Deepak T. Nair
Liang Tong
ORF1ab
Nidovirales
Epitranscriptomic sequencing
Small nucleolar RNA
SARS-related coronavirus
Exoribonuclease - Wikipedia
![XRN1 5-3 exoribonuclease 1 [Homo sapiens (human)] - Gene - NCBI](data:image/png;base64,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)
XRN1 5'-3' exoribonuclease 1 [Homo sapiens (human)] - Gene - NCBI
Network Portal - Function Oligoribonuclease (3'-|5' exoribonuclease)
REACTOME MRNA DECAY BY 3 TO 5 EXORIBONUCLEASE
Algorithmische Bioinformatik
The clinical and immunogenetic features of patients with autoantibodies to the nucleolar antigen PM-Scl
Redefining the invertebrate RNA virosphere | Nature
SWISS-MODEL Template Library | 4ro1
Rexo5 MGI Mouse Gene Detail - MGI:1919402 - RNA exonuclease 5
컨텐츠 | Nature Portfolio
Alumni - Biochemistry & Molecular Biology - Doctor of Philosophy(Ph.D.) - Graduate Education - Education - University of...
IJMS | Free Full-Text | Possible Pathogenesis and Prevention of Long COVID: SARS-CoV-2-Induced Mitochondrial Disorder
CATH Domain 1uk3B01
EXOSC4 Polyclonal Antibody (PA5-117154)
MMRRC:040067-MU
dhp1 gene cDNA ORF clone, Schizosaccharomyces pombe(fission yeast) - GenScript
XRN2 (human)
Template:Kinases - wikidoc
Publications | Crick
Dis3 | Knockout Mouse | Research Models | Taconic Biosciences
Viruses | Free Full-Text | Mutagenic Effects of Ribavirin on Hepatitis E Virus-Viral Extinction versus Selection of Fitness...
Translation/modification/RNA decay links | IGBMC
Publications scientifiques | IGBMC
MPD: Genes and genomic regions
ZR small-RNA PAGE Recovery Kit
SELECTBIO - Lab-on-a-Chip and Microfluidics Asia 2023 Agenda
YRC Public Data Repository - Gene Ontology GO Protein Search Results
RPP14 Antibody (NBP1-80965): Novus Biologicals
RCSB PDB - 6D6R: Human nuclear exosome-MTR4 RNA complex - composite map after focused reconstructionDIS31
- The structure reveals an RNA-engaged helicase atop the non-catalytic core, with RNA captured within the central channel and DIS3 exoribonuclease active site. (rcsb.org)
MRNA1
- Schizosaccharomyces pombe 5'-3' exoribonuclease Dhp1 (dhp1), mRNA. (genscript.com)
RNAs3
- An 3'-5'-exoribonuclease that specifically recognizes RNAs. (expasy.org)
- Exoribonuclease Nibbler was identified to module Piwi-interacting RNAs (piRNAs). (zymoresearch.com)
- Our data support the wide distribution of previously experimentally characterized exoribonuclease resistant RNAs (xrRNAs) within tick-borne and no-known-vector flaviviruses and provide evidence for the existence of a cascade of duplicated RNA structures within insect-specific flaviviruses. (nih.gov)
Polymerase2
- The nidovirus 3'-5' exoribonuclease (ExoN) domain may enhance the fidelity of RNA synthesis by correcting nucleotide incorporation errors made by the RNA-dependent RNA polymerase. (expasy.org)
- Subtle structural differences of nucleotide analogs may impact SARS-CoV-2 RNA-dependent RNA polymerase and exoribonuclease activity. (cdc.gov)
XRN12
MiRNA1
- Exoribonucleases are involved in the degradation of many different RNA species, including messenger RNA, transfer RNA, ribosomal RNA and miRNA. (wikipedia.org)
Exosome complex2
- Exoribonucleases can be single proteins (such as RNase D or RNase PH) but also can be complexes of multiple proteins, such as the exosome complex (in which four of the major exoribonuclease families are represented). (wikipedia.org)
- Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. (thermofisher.com)
Subunit1
- This gene encodes a subunit of ribonuclease P and has 3' to 5' exoribonuclease activity. (novusbio.com)
Exonuclease1
- An exoribonuclease is an exonuclease ribonuclease, which are enzymes that degrade RNA by removing terminal nucleotides from either the 5' end or the 3' end of the RNA molecule. (wikipedia.org)
Phosphorolytic2
- Exoribonucleases can use either water to cleave the nucleotide-nucleotide bond (which is called hydrolytic activity) or inorganic phosphate (which is called phosphorolytic activity). (wikipedia.org)
- Hydrolytic exoribonucleases are classified under EC number 3.1 and phosphorolytic exoribonucleases under EC number 2.7.7. (wikipedia.org)
Xrn21
- Canis lupus familiaris 5'-3' exoribonuclease 2 (XRN2), mRNA. (genscript.com)
Nsp145
- Identifying SARS-CoV-2 antiviral compounds by screening for small molecule inhibitors of nsp14/nsp10 exoribonuclease. (figshare.com)
- With the aim to identify novel SARS-CoV-2 antivirals, we have purified the exoribonuclease/methyltransferase (nsp14) and its cofactor (nsp10) and developed biochemical assays compatible with high-throughput approaches to screen for exoribonuclease inhibitors. (figshare.com)
- We have screened a library of over 5000 commercial compounds and identified patulin and aurintricarboxylic acid (ATA) as inhibitors of nsp14 exoribonuclease in vitro. (figshare.com)
- 2022. Activation of the SARS-CoV-2 NSP14 3'-5' exoribonuclease by NSP10 and response to antiviral inhibitors. (nih.gov)
- Non-structural protein 10 (nsp10) is a conserved stimulator of two enzymes crucial for viral replication, nsp14 and nsp16, exhibiting exoribonuclease and methyltransferase activities. (rcsb.org)
Enzymes2
- An exoribonuclease is an exonuclease ribonuclease, which are enzymes that degrade RNA by removing terminal nucleotides from either the 5' end or the 3' end of the RNA molecule. (wikipedia.org)
- Enzymes that remove nucleotides from the 5' end are called 5'-3' exoribonucleases, and enzymes that remove nucleotides from the 3' end are called 3'-5' exoribonucleases. (wikipedia.org)
DIS3L22
Polynucleotide2
- RNase E or R interacts with the phosphate-dependent exoribonuclease polynucleotide phosphorylase, DEAD-box helicases, and additional factors in the RNA-degrading complex. (kegg.jp)
- Abstract Polynucleotide phosphorylase (PNPase) can be an important mitochondria-localized exoribonuclease implicated in multiple natural processes and individual disorders. (bioskinrevive.com)
Protein1
- Results suggest that the RNase D family, which includes Werner syndrome protein and the 100 kDa antigenic component of the human polymyositis scleroderma (PMSCL) autoantigen, is a 3'-->5' exoribonuclease structurally and functionally related to the 3'-->5' exodeoxyribonuclease domain of DNA polymerases. (embl.de)
ERI11
- ERI1 exoribonuclease famil. (gsea-msigdb.org)
RNase4
- Exoribonucleases can be single proteins (such as RNase D or RNase PH) but also can be complexes of multiple proteins, such as the exosome complex (in which four of the major exoribonuclease families are represented). (wikipedia.org)
- RNase R is an E. coli exoribonuclease which exhibits 3' to 5' exonuclease activity, efficiently digesting nearly all linear RNA species. (mclab.com)
- Acts as an exoribonuclease (RNase) responsible for trimming the poly(U) tract of the last nucleotides in the pre-U6 snRNA molecule, leading to the formation of mature U6 snRNA 3' end-terminated with a 2',3'-cyclic phosphate. (expasy.org)
- Acts as an exoribonuclease (RNase) responsible for trimming the poly(U) tract of the last nucleotides in the pre-U6 snRNA molecule, leading to the formation of mature U6 snRNA. (expasy.org)
Degradation4
- Exoribonucleases are involved in the degradation of many different RNA species, including messenger RNA, transfer RNA, ribosomal RNA and miRNA. (wikipedia.org)
- With the recent discovery of roles for microRNAs in gene expression, it was reported that the HCV RNA genome subverts liver-specific microRNA miR-122 to protect its 5' end from degradation by host cell exoribonucleases. (medscape.com)
- Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. (thermofisher.com)
- 5 exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. (nih.gov)
Mitochondrial1
- The yeast mitochondrial degradosome (mtEXO) is an NTP-dependent exoribonuclease involved in mitochondrial RNA metabolism. (gzsys.org.cn)
Poly1
- Molecular function: poly(U)-specific exoribonuclease activity, producing 3' uridine cyclic phosphate ends. (expasy.org)
Activity3
- Enables 3'-5'-exoribonuclease activity. (nih.gov)
- 2019). Whether such a specific activity exists in organisms that lack Orn-type exoribonucleases remained unclear. (cornell.edu)
- The structures, together with comparative genomic analyses of the phylogeny of DEDD-type exoribonucleases, indicate convergent evolution as the mechanism of how dinucleotidase activity emerged repeatedly in various organisms. (cornell.edu)
Yeast1
- Recently, it was discovered that the PM/Scl complex is the human counterpart of the yeast ( Saccharomyces cerevisiae ) exosome, which is an RNA-processing complex consisting of 11 3' → 5' exoribonucleases. (biomedcentral.com)
Function1
- What is the function of Exoribonuclease? (ventolaphotography.com)