Polynucleotide phosphorylase functions both as a 3' right-arrow 5' exonuclease and a poly(A) polymerase in Escherichia coli.
about
Mammalian polynucleotide phosphorylase is an intermembrane space RNase that maintains mitochondrial homeostasisAnalysis of the human polynucleotide phosphorylase (PNPase) reveals differences in RNA binding and response to phosphate compared to its bacterial and chloroplast counterpartsStable PNPase RNAi silencing: its effect on the processing and adenylation of human mitochondrial RNADegradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'Human mitochondrial SUV3 and polynucleotide phosphorylase form a 330-kDa heteropentamer to cooperatively degrade double-stranded RNA with a 3'-to-5' directionalityRNase J is required for processing of a small number of RNAs in Rhodobacter sphaeroidesRNA polyadenylation in Archaea: not observed in Haloferax while the exosome polynucleotidylates RNA in Sulfolobus.Polyadenylation of ribosomal RNA in human cellsPolynucleotide phosphorylase functions as both an exonuclease and a poly(A) polymerase in spinach chloroplastsKinetics of polynucleotide phosphorylase: comparison of enzymes from Streptomyces and Escherichia coli and effects of nucleoside diphosphatesRNA-specific ribonucleotidyl transferasesDomain analysis of the chloroplast polynucleotide phosphorylase reveals discrete functions in RNA degradation, polyadenylation, and sequence homology with exosome proteinsRegulation and functions of bacterial PNPaseThe interplay of Hfq, poly(A) polymerase I and exoribonucleases at the 3' ends of RNAs resulting from Rho-independent termination: A tentative modelCrystal structure of Escherichia coli PNPase: Central channel residues are involved in processive RNA degradationCrystal Structure of Escherichia coli Polynucleotide Phosphorylase Core Bound to RNase E, RNA and Manganese: Implications for Catalytic Mechanism and RNA Degradosome AssemblyCrystal structure of human polynucleotide phosphorylase: insights into its domain function in RNA binding and degradationUncoupling the roles of the SUV3 helicase in maintenance of mitochondrial genome stability and RNA degradation.A new function in translocation for the mitochondrial i-AAA protease Yme1: import of polynucleotide phosphorylase into the intermembrane space.The archaeal exosome core is a hexameric ring structure with three catalytic subunitsEndonucleolytic cleavages by RNase E generate the mature 3' termini of the three proline tRNAs in Escherichia coliPolynucleotide phosphorylase has an impact on cell biology of Campylobacter jejuni.Chloroplast PNPase exists as a homo-multimer enzyme complex that is distinct from the Escherichia coli degradosomeRNase activity of polynucleotide phosphorylase is critical at low temperature in Escherichia coli and is complemented by RNase IIAirpnp: Auto- and Integrated Regulation of Polynucleotide Phosphorylase.Landscape of RNA polyadenylation in E. coli.Inhibition of homologous phosphorolytic ribonucleases by citrate may represent an evolutionarily conserved communicative link between RNA degradation and central metabolism.Repair of the tRNA-like CCA sequence in a multipartite positive-strand RNA virus.Helicase SUV3, polynucleotide phosphorylase, and mitochondrial polyadenylation polymerase form a transient complex to modulate mitochondrial mRNA polyadenylated tail lengths in response to energetic changes.Addition of poly(A) and heteropolymeric 3' ends in Bacillus subtilis wild-type and polynucleotide phosphorylase-deficient strains.A phylogeny of bacterial RNA nucleotidyltransferases: Bacillus halodurans contains two tRNA nucleotidyltransferasesThe response regulator SprE (RssB) is required for maintaining poly(A) polymerase I-degradosome association during stationary phase.Selective mRNA degradation by polynucleotide phosphorylase in cold shock adaptation in Escherichia coliRNA quality control: degradation of defective transfer RNA(p)ppGpp inhibits polynucleotide phosphorylase from streptomyces but not from Escherichia coli and increases the stability of bulk mRNA in Streptomyces coelicolor.RhlB helicase rather than enolase is the beta-subunit of the Escherichia coli polynucleotide phosphorylase (PNPase)-exoribonucleolytic complex.The Streptomyces coelicolor polynucleotide phosphorylase homologue, and not the putative poly(A) polymerase, can polyadenylate RNA.mRNA decay in Escherichia coli comes of age.Sequence motifs that distinguish ATP(CTP):tRNA nucleotidyl transferases from eubacterial poly(A) polymerases.Proteomic profiling of a robust Wolbachia infection in an Aedes albopictus mosquito cell line.
P2860
Q24302448-FDDEDB5C-BBFC-4A92-B11A-DEB089BB55BCQ24303834-86A0F7B2-C6DB-4351-8796-A9C17A2C5A29Q24303855-B8164420-0DD0-45A5-830D-641248E227B5Q24305376-DA2893B1-6F09-4CB7-B29D-3B146461309BQ24337635-54BFBDB2-F0B5-4D69-98FF-F66734E71C8FQ24489997-A94D0E1F-372E-4D46-8C78-EB8D4720E278Q24539131-C358F1C6-133E-422F-AE5F-09A0ADFB6829Q24546450-0D7E126C-7E91-4B50-8074-8EB9E60073E8Q24550883-8415F4DF-DD20-4859-AE3F-530CEA27FA01Q24657805-25E40475-2A0C-46FE-9081-0D092438DFA1Q24676059-CC175F23-A0D3-469F-B77F-460A9DB88533Q24682917-74CE31E3-BF6B-4EF5-89C8-2BD6E9CEE546Q26770015-54D83547-2DD2-48AF-AE96-8637F1F8A05BQ26852007-81F71E2A-C033-415D-A772-8DBACF1B25A9Q27652277-06394EB9-C338-4F53-85B2-CA679C2F7E91Q27654474-D92FE7CF-D6A7-43F6-A985-545AE7796653Q27676507-11315C2C-681E-4E30-894A-A1CF8C7D6D78Q27932248-4480738B-C812-4DB2-89A8-B4301706FAD3Q27932867-EB6D8646-04F0-4EE7-A33C-84C55D87304CQ28256090-3611D694-5ED1-48ED-8290-54FA518FD759Q28817520-5DB78C19-8453-4A41-9720-9111925E14F9Q30425436-DF8CD279-B0FA-4F61-9908-3F59B6A7B3ECQ30447072-08EFD27C-5516-4738-B43C-22BA8CB56ED7Q33349686-00737A2B-3DDE-4A8C-87D5-332BF259D21CQ33361659-A9F3DFEE-AA90-43C5-BD3B-29E5B266B9BFQ33557573-C1357065-BCBC-4122-96FA-7562D4429F00Q33635838-19CCAEA5-B7CD-4CD3-944F-766C5E91C19CQ33718671-A7F80A65-CBCF-4B22-B186-BF88775E37DAQ33761176-284EBCC8-2FB4-4ED8-BF3A-9C6C3FF529CAQ33885757-3295DC90-5B5F-4B29-92F1-6D4509707572Q33937742-18A8EC71-E979-48A5-87E2-17FECA5D6EC5Q33962944-7D525276-C670-4C56-AFF7-C07C1F714721Q34011345-2404D11F-3F60-444C-93DF-8153BD169EB3Q34086017-9021E077-EA1C-4219-A62F-C7D78E670ABFQ34119119-F826E48B-6DC5-448B-9A7D-FDBE63986AB4Q34120489-02424DB3-A53A-4DBA-B456-2EFA4264DEDBQ34232403-08FD52D6-3A48-4139-AAF9-50F32C187E52Q34317343-DFA6B821-9A38-43A3-96B8-3605F8522F6CQ34365762-CE9461F5-7D32-4D2F-BE20-176DAE7D7BA7Q34422402-C054950F-DA95-4E4C-BD77-75B7F8ECAAFA
P2860
Polynucleotide phosphorylase functions both as a 3' right-arrow 5' exonuclease and a poly(A) polymerase in Escherichia coli.
description
2000 nî lūn-bûn
@nan
2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Polynucleotide phosphorylase f ...... olymerase in Escherichia coli.
@ast
Polynucleotide phosphorylase f ...... olymerase in Escherichia coli.
@en
type
label
Polynucleotide phosphorylase f ...... olymerase in Escherichia coli.
@ast
Polynucleotide phosphorylase f ...... olymerase in Escherichia coli.
@en
prefLabel
Polynucleotide phosphorylase f ...... olymerase in Escherichia coli.
@ast
Polynucleotide phosphorylase f ...... olymerase in Escherichia coli.
@en
P2860
P356
P1476
Polynucleotide phosphorylase f ...... olymerase in Escherichia coli.
@en
P2093
B K Mohanty
S R Kushner
P2860
P304
11966-11971
P356
10.1073/PNAS.220295997
P407
P577
2000-10-01T00:00:00Z