Putative 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. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding pervasive transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3 untranslated regions, and in RNA surveillance pathways, preventing
Polynucleotide Phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3 to 5 exoribonuclease activity and a 3-terminal oligonucleotide polymerase activity.[2] That is, it dismantles the RNA chain starting at the 3 end and working toward the 5 end.[1] It also synthesizes long, highly heteropolymeric tails in vivo. It accounts for all of the observed residual polyadenylation in strains of Escherichia coli missing the normal polyadenylation enzyme.[1] Discovered by Marianne Grunberg-Manago working in Severo Ochoas lab in 1955, the RNA-polymerization activity of PNPase was initially believed to be responsible for DNA-dependent synthesis of messenger RNA, a notion that got disproved by the late 1950s.[3][4] It is involved in mRNA processing and degradation in bacteria, plants,[5] and in humans.[6] In humans, the enzyme is encoded by the PNPT1 gene. In its active form, the protein forms a ring structure consisting of three PNPase molecules. Each PNPase molecule consists of two ...
Degradation of mRNA is a highly regulated step important for proper gene expression. Degradation of eukaryotic mRNA is initiated by shortening of the 3 end located poly(A) tail. Poly(A)-specific ribonuclease (PARN) is an oligomeric enzyme that degrades the poly(A) tail with high processivity. A unique property of PARN is its ability to interact not only with the poly(A) tail but also with the 5 end located mRNA cap structure. A regulatory role in protein synthesis has been proposed for PARN based on its ability to bind the cap that is required for efficient initiation of eukaryotic mRNA translation. Here we have investigated how the cap structure influences PARN activity and how PARN binds the cap. We show that the cap activates PARN and enhances the processivity of PARN. Further we show that the cap binding complex (CBC) inhibits PARN activity through a protein-protein interaction. To investigate the cap binding property of PARN, we identified the cap binding site at the molecular level using ...
Background Deadenylation regulates RNA function and fate. Poly(A)-specific ribonuclease (PARN) is a deadenylase that processes mRNAs and non-coding RNA. Little is known about the biological significance of germline mutations in PARN. Methods We identified mutations in PARN in patients with haematological and neurological manifestations. Genomic, biochemical and knockdown experiments in human marrow cells and in zebrafish have been performed to clarify the role of PARN in the human disease. Results We identified large monoallelic deletions in PARN in four patients with developmental delay or mental illness. One patient in particular had a severe neurological phenotype, central hypomyelination and bone marrow failure. This patient had an additional missense mutation on the non-deleted allele and severely reduced PARN protein and deadenylation activity. Cells from this patient had impaired oligoadenylation of specific H/ACA box small nucleolar RNAs. Importantly, PARN-deficient patient cells ...
Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs. The amino acid sequence of poly(A)-specific ribonuclease shows homology to the RNase D family of 3-exonucleases. The protein appears to be localized in both the nucleus and the cytoplasm. It is not stably associated with polysomes or ribosomal subunits.[2] Hereditary mutations in PARN lead to the bone marrow failure disease Dyskeratosis Congenita which is caused by defective telomerase RNA processing and degradation in patients.[3][4][5][6][7][8][9] ...
Obesity affects a significant number of Americans and greatly increases the risk of developing cardiovascular disease, type-II diabetes, fatty liver disease, and certain cancers. Understanding how obesity is regulated opens up new avenues of pharmacological interventions to treat obesity, concurrently reducing the risk of co-morbidities. Nocturnin (NOCT) is broadly expressed enzyme with exoribonuclease activity in in vitro assays and a repressive function against reporter RNAs in vivo. These observations are consistent with a function in RNA decay. Mice lacking NOCT are resistant to diet-induced obesity and other studies have observed a role for NOCT in regulating intestinal trafficking of dietary fats and promoting adipogenesis. These observations suggest that NOCT may have a novel role in the regulation of lipid metabolism by targeting mRNAs for degradation. Though the broader physiological effects of NOC gene deletion have been described, discovering the molecular function of NOC remains an ...
EXD3 Full-Length MS Protein Standard (NP_060290), Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine, was produced in human 293 cells (HEK293) with fully chemically defined cell culture medium to obtain incorporation efficiency at Creative-Proteomics. Possesses 3-5 exoribonuclease activity. Required for 3-end trimming of AGO1-bound miRNAs.
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Previous works in the budding yeast S. cerevisiae and the fission yeast S. pombe have revealed that aslncRNAs are globally low abundant as they are extensively degraded by RNA surveillance machineries. For instance, the nuclear exosome targets a class of lncRNAs referred to as CUTs (Wyers et al, 2005; Neil et al, 2009; Xu et al, 2009), whereas the cytoplasmic 5′-3′ exoribonuclease Xrn1 degrades the so-called XUTs (Van Dijk et al, 2011), both types of transcripts being mainly antisense to protein-coding genes. However, this classification into CUTs and XUTs is not exclusive, some aslncRNAs being cooperatively targeted by the two RNA decay pathways. In fission yeast, an additional class of aslncRNAs (DUTs) was recently identified. DUTs accumulate in the absence of the ribonuclease III Dicer (Atkinson et al, 2018), highlighting the role of Dicer and RNAi in the control of aslncRNAs expression in fission yeast. This class of transcripts is absent in S. cerevisiae, which has lost the RNAi system ...
Project A1: The role of th poly(A) specific ribonuclease (PARN) during stress Regulation of RNA stability plays an important role in the regulation of gene expression. The first and often rate limiting step in mRNA decay is the removal of the poly(A)tail. The poly(A)-specific ribonuclease (PARN) is an enzyme that catalyzes the removal of the poly(A)tail in vitro and can probably influence gene expression posttranscriptionally. But not much is known about the in vivo function of PARN in mammalian cells. Using microarray analysis we could identify several potential PARN substrates and now Im going to clarify the role of this enzyme in mammalian cells. Supervisor: Prof. Wahle contact ...
Exosome-RNA.com is a place to find the latest research and industry news and information about exosome RNA. The exosome complex is present in the cytoplasm, nucleus and especially the nucleolus. Substrates of the exosome include messenger RNA, ribosomal RNA, and many species of small RNAs. The exosome has an exoribonucleolytic function, meaning it degrades RNA starting at one end (the 3′ end in this case), and in eukaryotes also an endoribonucleolytic function, meaning it cleaves RNA at sites within the molecule. - from wikipedia. ...
Genetic information processingTranscriptionDegradation of RNAVacB and RNase II family 3-5 exoribonucleases (TIGR00358; EC 3.1.13.1; HMM-score: 16.6) ...
5-3 decay is the major mRNA decay pathway in many eukaryotes, including trypanosomes. After deadenylation, mRNAs are decapped by the nudix hydrolase DCP2 of the decapping complex and finally degraded by the 5-3 exoribonuclease. Uniquely, trypanosomes lack homologues to all subunits of the decapping complex, while deadenylation and 5-3 degradation are conserved. Here, I show that the parasites use an ApaH-like phosphatase (ALPH1) as their major mRNA decapping enzyme. The protein was recently identified as a novel trypanosome stress granule protein and as involved in mRNA binding. A fraction of ALPH1 co-localises exclusively with the trypanosome 5-3 exoribonuclease XRNA to a special granule at the posterior pole of the cell, indicating a connection between the two enzymes. RNAi depletion of ALPH1 is lethal and causes a massive increase in total mRNAs that are deadenylated, but have not yet started 5-3 decay. These data suggest that ALPH1 acts downstream of deadenylation and upstream of ...
During pre-mRNA splicing, exons in the primary transcript are precisely connected to generate an mRNA. Intron lariat RNAs are formed as by-products of this process. In addition, some exonic circular RNAs (circRNAs) may also result from exon skipping as by-products. Lariat RNAs and circRNAs are both RNase R resistant RNAs. RNase R is a strong 3 to 5 exoribonuclease, which efficiently degrades linear RNAs, such as mRNAs and rRNAs; therefore, the circular parts of lariat RNAs and the circRNAs can be segregated from eukaryotic total RNAs by their RNase R resistance. Thus, RNase R resistant RNAs could provide unexplored splicing information not available from mRNAs. Analyses of these RNAs identified repeating splicing phenomena, such as re-splicing of mature mRNAs and nested splicing. Moreover, circRNA might function as microRNA sponges. There is an enormous variety of endogenous circRNAs, which are generally synthesized in cells and tissues.
U6 snRNA phosphodiesterase; Phosphodiesterase responsible for the U6 snRNA 3 end processing. 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 (279 aa ...
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Complete information for PAN3 gene (Protein Coding), PAN3 Poly(A) Specific Ribonuclease Subunit, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
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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. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding pervasive transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3 untranslated regions, and in RNA surveillance pathways, ...
The autoantigenic polymyositis/scleroderma (PM/Scl) complex was recently shown to be the human homologue of the yeast exosome, which is an RNA-processing complex. Our aim was to assess whether, in addition to targeting the known autoantigens PM/Scl-100 and PM/Scl-75, autoantibodies also target recently identified components of the PM/Scl complex. The prevalence of autoantibodies directed to six novel human exosome components (hRrp4p, hRrp40p, hRrp41p, hRrp42p, hRrp46p, hCsl4p) was determined in sera from patients with idiopathic inflammatory myopathy (n = 48), scleroderma (n = 11), or the PM/Scl overlap syndrome (n = 10). The sera were analyzed by enzyme-linked immunosorbent assays and western blotting using the affinity-purified recombinant proteins. Our results show that each human exosome component is recognized by autoantibodies. The hRrp4p and hRrp42p components were most frequently targeted. The presence of autoantibodies directed to the novel components of the human exosome was correlated with
TY - JOUR. T1 - An essential function for the phosphate-dependent exoribonucleases RNase PH and polynucleotide phosphorylase. AU - Zhou, Zhihua. AU - Deutscher, Murray P.. PY - 1997/7. Y1 - 1997/7. N2 - Escherichia coli cells lacking both polynucleotide phosphorylase (PNPase) and RNase PH, the only known P1-dependent exoribonucleases, were previously shown to grow slowly at 37°C and to display a dramatically reduced level of tRNA(Tryrsu3+) suppressor activity. Here we show that the RNase PH-negative, PNP-negative double-mutant strain actually displays a reversible cold-sensitive phenotype and that tRNA biosynthesis is normal. In contrast, ribosome structure and function are severely affected, particularly at lower temperatures. At 31°C, the amount of 50S subunit is dramatically reduced and 23S rRNA is degraded. Moreover, cells that had been incubated at 42°C immediately cease growing and synthesizing protein upon a shift to 31°C, suggesting that the ribosomes synthesized at the higher ...
In this study, the importance of the RPH domains in mediating the characteristic phenotypic changes induced by hPNPaseold-35 is firmly established. We observed that the presence of at least one RPH domain is required for the functional activity of the protein and either of the domains is as potent as the full-length molecule. This contrasts with bacterial PNPase in which mutation in the key residues in either of the RPH domains inhibits catalytic activity (19). However, our result is comparable to chloroplast PNPase in which the first RPH domain alone (comparable to our ΔRPH2 construct) is highly active enzymatically (40). Although the second RPH domain (our ΔRPH1) of the chloroplast has low RNA degradation activity of nonpolyadenylated RNA, it has high activity for polyadenylated RNA (40), which explains the efficiency of the ΔRPH1 construct in degrading human polyadenylated mRNAs. The RPH domains themselves can bind to RNA, and the PNPase domain is also involved in RNA binding, which ...
Escherichia coli polynucleotide phosphorylase (PNPase) is generally believed to be involved in mRNA degradation via its 3$\sp\prime$ to 5$\sp\prime$ exoribonuclease activity. However, there are many unexplained observations related to the physiological role of this enzyme. The projects conducted in this thesis are aimed at understanding more about the in vivo function of PNPase. Two approaches were employed to try to achieve this goal. First, a biochemical approach involving the purification of PNPase associated proteins was used. Specifically, the previously documented $\beta$ subunit present in the pentameric form of PNPase was examined as an initial step toward understanding the mechanism and possibly the regulation of PNPase catalysis. Second, a genetic approach was undertaken which focused on characterization of mutant strains lacking PNPase in combination with other known enzymes involved in RNA metabolism, in particular, tRNA nucleotidyltransferase, poly(A) polymerase and RNase PH.^ From the
TY - JOUR. T1 - Catalytic properties of RNase BN/RNase Z from Escherichia coli. RNase BN is both an exo- and endoribonuclease. AU - Dutta, Tanmay. AU - Deutscher, Murray P. PY - 2009/6/5. Y1 - 2009/6/5. N2 - Processing of the 3′ terminus of tRNA in many organisms is carried out by an endoribonuclease termed RNase Z or 3′-tRNase, which cleaves after the discriminator nucleotide to allow addition of the universal- CCA sequence. In some eubacteria, such as Escherichia coli, the -CCA sequence is encoded in all known tRNA genes. Nevertheless, an RNase Z homologue (RNase BN) is still present, even though its action is not needed for tRNA maturation. To help identify which RNA molecules might be potential substrates for RNase BN, we carried out a detailed examination of its specificity and catalytic potential using a variety of synthetic substrates. We show here that RNase BN is active on both double- and single-stranded RNA but that duplex RNA is preferred. The enzyme displays a profound base ...
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Extensive bioinformatics analysis suggests that the stability and function of protein complexes are maintained throughout evolution by coordinated changes (co-evolution) of complex subunits. Yet, relatively little is known regarding the actual dynamics of such processes and the functional implications of co-evolution within protein complexes, since most of the bioinformatics predictions were not analyzed experimentally. Here, we describe a systematic experimental approach that allows a step-by-step observation of the co-evolution process in protein complexes. The exosome complex, an essential complex exhibiting a 3→5 RNA degradation activity, served as a model system. In this study, we show that exosome subunits diverged very early during fungal evolution. Interestingly, we found that despite significant differences in conservation between Rrp41 and Mtr3 both subunits exhibit similar divergence pattern and co-evolutionary behavior through fungi evolution. Activity analysis of mutated ...
Children, adolescents and young adults with high risk relapsed or treatment refractory neuroblastoma (rNB) represent a group of patients with dismal prognosis for whom a recommended standard salvage therapy is currently not available.. The multimodal metronomic approach combining molecular targeted drugs (rapamycin and dasatinib) with conventional chemotherapy (irinotecan and temozolomide) will be investigated in a randomized fashion as new treatment strategy for patients with rNB. The intention is to assess the therapeutic benefit of molecular targeted drugs for the treatment of rNB.. The combination of irinotecan and temozolomide showed activity in the treatment of several solid organ tumors, brain tumors and neuroblastoma. In one study rNB patients received a median of 5 courses of 5 days irinotecan and temozolomide every 3 to 4 weeks with a cumulative dose of 35% lower than in the RIST design. 33% had disease regression with 8% CR or PR. A phase II study in rNB also using irinotecan and ...
Germline coding mutations in different telomere-related genes have been linked to autosomal-dominant familial pulmonary fibrosis. Individuals with these inherited mutations demonstrate incomplete penetrance of clinical phenotypes affecting the lung, blood, liver, skin, and other organs. Here, we describe the somatic acquisition of promoter mutations in telomerase reverse transcriptase (TERT) in blood leukocytes of approximately 5% of individuals with inherited loss-of-function coding mutations in TERT or poly(A)-specific ribonuclease (PARN), another gene linked to telomerase function. While these promoter mutations were initially identified as oncogenic drivers of cancer, individuals expressing the mutations have no history of cancer. Neither promoter mutation was found in population-based cohorts of similar or advanced age. The TERT promoter mutations were found more frequently in cis with the WT allele than the TERT coding sequence mutation. EBV-transformed lymphoblastoid B cell lines (LCLs) ...
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bin/bash # This script is designed to help you clean your computer from unneeded # packages. The script will find all packages that no other installed package # depends on. It will output this list of packages excluding any you have # placed in the ignore list. You may browse through the scripts output and # remove any packages you do not need. # Enter groups and packages here which you know you wish to keep. They will # not be included in the list of unrequired packages later. ignoregrp="base base-devel" ignorepkg="" # Temporary file locations tmpdir=/tmp ignored=$tmpdir/ignored installed=$tmpdir/installed # Generate list of installed packages and packages you wish to keep. echo $(pacman -Sg$ignoregrp , awk {print $2})$ignorepkg , tr \n , sort , uniq , $ignored pacman -Qq , sort ,$installed # Do not loop packages you are keeping loop=$(comm -13$ignored $installed) # Check each remaining package. If package is not required by anything and # is not on your ignore list, print the ... bin/bash # This script is designed to help you clean your computer from unneeded # packages. The script will find all packages that no other installed package # depends on. It will output this list of packages excluding any you have # placed in the ignore list. You may browse through the scripts output and # remove any packages you do not need. # Enter groups and packages here which you know you wish to keep. They will # not be included in the list of unrequired packages later. ignoregrp="base base-devel" ignorepkg="" # Temporary file locations tmpdir=/tmp ignored=$tmpdir/ignored installed=$tmpdir/installed # Generate list of installed packages and packages you wish to keep. echo$(pacman -Sg $ignoregrp , awk {print$2}) $ignorepkg , tr \n , sort , uniq ,$ignored pacman -Qq , sort , $installed # Do not loop packages you are keeping loop=$(comm -13 $ignored$installed) # Check each remaining package. If package is not required by anything and # is not on your ignore list, print the ...
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casSAR Dugability of Q89WK4 | rph | Ribonuclease PH - Also known as RNPH_BRADU, rph. Phosphorolytic 3-5 exoribonuclease that plays an important role in tRNA 3-end maturation. Removes nucleotide residues following the 3-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. Homohexameric ring arranged as a trimer of dimers.
casSAR Dugability of C3K479 | rph | Ribonuclease PH - Also known as RNPH_PSEFS, rph. Phosphorolytic 3-5 exoribonuclease that plays an important role in tRNA 3-end maturation. Removes nucleotide residues following the 3-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. Homohexameric ring arranged as a trimer of dimers.
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Background: Eukaryotic cells have developed surveillance mechanisms to prevent the expression of aberrant transcripts. An early surveillance checkpoint acts at the transcription site and prevents the release of mRNAs that carry processing defects. The exosome subunit Rrp6 is required for this checkpoint in Saccharomyces cerevisiae, but it is not known whether Rrp6 also plays a role in mRNA surveillance in higher eukaryotes.. Methodology/Principal Findings: We have developed an in vivo system to study nuclear mRNA surveillance in Drosophila melanogaster. We have produced S2 cells that express a human β-globin gene with mutated splice sites in intron 2 (mut β-globin). The transcripts encoded by the mut β-globin gene are normally spliced at intron 1 but retain intron 2. The levels of the mut β-globin transcripts are much lower than those of wild type (wt) ß-globin mRNAs transcribed from the same promoter. We have compared the expression of the mut and wt β-globin genes to investigate the ...
Strand exchange protein 1 (SEP1) homolog was reported as a human gene responsive to stimulation by glial cell-derived neurotrophic factor (GDNF) in neuroblastoma cells. It was subsequently characterized as the human homolog to yeast XRN1 protein, a 5-3 exoribonuclease. SEP1 is involved in mRNA degradation, and in a variety of other nuclear and cytoplasmic functions. It may also act as a tumor suppressor protein in osteogenic sarcoma (OGS). SEP1 is also known as XRN1 and 5-3 exoribonuclease 1.. ...
Contents. EC 3.1.1 Carboxylic Ester Hydrolases. EC 3.1.2 Thioester Hydrolases. EC 3.1.3 Phosphoric Monoester Hydrolases. EC 3.1.4 Phosphoric Diester Hydrolases. EC 3.1.5 Triphosphoric Monoester Hydrolases. EC 3.1.6 Sulfuric Ester Hydrolases. EC 3.1.7 Diphosphoric Monoester Hydrolases. EC 3.1.8 Phosphoric Triester Hydrolases. EC 3.1.11 Exodeoxyribonucleases Producing 5-Phosphomonoesters. EC 3.1.12 Exodeoxyribonucleases Producing 3-Phosphomonoesters. EC 3.1.13 Exoribonucleases Producing 5-Phosphomonoesters. EC 3.1.14 Exoribonucleases Producing 3-Phosphomonoesters. EC 3.1.15 Exonucleases Active with either Ribo- or Deoxyribonucleic Acids and Producing 5-Phosphomonoesters. EC 3.1.16 Exonucleases Active with either Ribo- or Deoxyribonucleic Acids and Producing 3-Phosphomonoesters. EC 3.1.21 Endodeoxyribonucleases Producing 5-Phosphomonoesters. EC 3.1.22 Endodeoxyribonucleases Producing 3-Phosphomonoesters. EC 3.1.23 Site Specific Endodeoxyribonucleases: Cleavage is Sequence Specific ...
Molecular mechanism of processive 3′ to 5′ RNA translocation in the active subunit of the RNA exosome complex. Recent experimental studies revealed structural details of 3′ to 5′ degradation of RNA molecules, performed byt he exosome complex. ssRNA is channeled through its multisubunit ring-like core into the active site tunnel of its key exonuclease subunit Rrp44, which acts both as an enzyme and a motor. Even in isolation, Rrp44 can pull and sequentially cleave RNA nucleotides, one at a time, without any external energy input and release a final 3−5 nucleotide long product. Using molecular dynamics simulations, we identify the main factors that control these processes. Our free energy calculations reveal that RNA transfer from solution into the active site of Rrp44 is highly favorable, but dependent on the length of the RNA strand. While RNA strands formed by 5 nucleotides or more correspond to a decreasing free energy along the translocation coordinate toward the cleavage site, a ...
Intracellular mRNA transport and local translation play a key role in neuronal physiology. Translationally repressed mRNAs are transported as a part of ribonucleoprotein (RNP) particles to distant dendritic sites, but the properties of different RNP particles and mechanisms of their repression and transport remain largely unknown. Here, we describe a new class of RNP-particles, the dendritic P-body-like structures (dlPbodies), which are present in the soma and dendrites of mammalian neurons and have both similarities and differences to P-bodies of non-neuronal cells. These structures stain positively for a number of P-body and microRNP components, a microRNA-repressed mRNA and some translational repressors. They appear more heterogeneous than P-bodies of HeLa cells, and they rarely contain the exonuclease Xrn1 but are positive for rRNA. These particles show motorized movements along dendrites and relocalize to distant sites in response to synaptic activation. Furthermore, Dcp1a is stably ...
Q504Q3: PAB-dependent poly(A)-specific ribonuclease subunit PAN2 {ECO:0000255,HAMAP-Rule:MF_03182}; hPan2; 3.1.13.4 {ECO:0000255,HAMAP-Rule:MF_03182}; Inactive ubiquitin carboxyl-terminal hydrolase 52 {ECO:0000255,HAMAP-Rule:MF_03182}; PAB1P-dependent poly(A)-nuclease {ECO:0000255,HAMAP-Rule:MF_03182}; PAN deadenylation complex catalytic subunit 2 {ECO:0000255,HAMAP-Rule:MF_03182 ...
Cohen D., Mechold U., Nevenzal H., Yarmiyhu Y., Randall T.E., Bay D.C., Rich J.D., Parsek M.R., Kaever V., Harrison J.J. and E. Banin. (2015). Oligoribonuclease is a central feature of c-di-GMP signalling in Pseudomonas aeruginosa. Proceedings of the National Academy of Sciences USA. pii: 201421450. DOI:10.1073/pnas.1421450112. This work was selected by Science Signaling (one of three Science Magazine daughter journals) as one of 2015 Signal Transduction Breakthroughs of the Year. ...