RNase E activity is conferred by a single polypeptide: overexpression, purification, and properties of the ams/rne/hmp1 gene product
about
ARD-1 cDNA from human cells encodes a site-specific single-strand endoribonuclease that functionally resembles Escherichia coli RNase EThe catalytic domain of RNase E shows inherent 3' to 5' directionality in cleavage site selectionard-1: a human gene that reverses the effects of temperature-sensitive and deletion mutations in the Escherichia coli rne gene and encodes an activity producing RNase E-like cleavagesRibonuclease E organizes the protein interactions in the Escherichia coli RNA degradosomeCharacterization of native and reconstituted exosome complexes from the hyperthermophilic archaeon Sulfolobus solfataricusSubstrate binding and active site residues in RNases E and G: role of the 5'-sensorMembrane binding of Escherichia coli RNase E catalytic domain stabilizes protein structure and increases RNA substrate affinity.Chloroplast PNPase exists as a homo-multimer enzyme complex that is distinct from the Escherichia coli degradosomeA human RNase E-like activity that cleaves RNA sequences involved in mRNA stability control.A binding factor for interleukin 2 mRNA.The Escherichia coli major exoribonuclease RNase II is a component of the RNA degradosome.Translation of the adhE transcript to produce ethanol dehydrogenase requires RNase III cleavage in Escherichia coliThe endoribonucleolytic N-terminal half of Escherichia coli RNase E is evolutionarily conserved in Synechocystis sp. and other bacteria but not the C-terminal half, which is sufficient for degradosome assemblyThe RNase E/G-type endoribonuclease of higher plants is located in the chloroplast and cleaves RNA similarly to the E. coli enzyme.Translation inhibitors stabilize Escherichia coli mRNAs independently of ribosome protection.Proteins associated with RNase E in a multicomponent ribonucleolytic complex.RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region.Evidence for an RNA binding region in the Escherichia coli processing endoribonuclease RNase E.Escherichia coli poly(A)-binding proteins that interact with components of degradosomes or impede RNA decay mediated by polynucleotide phosphorylase and RNase E.Two mutant forms of the S1/TPR-containing protein Rrp5p affect the 18S rRNA synthesis in Saccharomyces cerevisiae.Ribonuclease E is a 5'-end-dependent endonuclease.Determination of the catalytic parameters of the N-terminal half of Escherichia coli ribonuclease E and the identification of critical functional groups in RNA substrates.Biochemical and serological evidence for an RNase E-like activity in halophilic Archaea.RNase E polypeptides lacking a carboxyl-terminal half suppress a mukB mutation in Escherichia coliReconstitution of a minimal RNA degradosome demonstrates functional coordination between a 3' exonuclease and a DEAD-box RNA helicase.Roles of RNase E, RNase II and PNPase in the degradation of the rpsO transcripts of Escherichia coli: stabilizing function of RNase II and evidence for efficient degradation in an ams pnp rnb mutant.RNase E: still a wonderfully mysterious enzyme.Localization of riboproteins in a trypanosomatid mitochondrion.Roles of the 5'-phosphate sensor domain in RNase E.Analysis of the RNA degradosome complex in Vibrio angustum S14.The CafA protein required for the 5'-maturation of 16 S rRNA is a 5'-end-dependent ribonuclease that has context-dependent broad sequence specificity.Function in Escherichia coli of the non-catalytic part of RNase E: role in the degradation of ribosome-free mRNA.Processing of the rne transcript by an RNase E-independent amino acid-dependent mechanism.Modulation of the activity of RNase E in vitro by RNA sequences and secondary structures 5' to cleavage sites.Differential sensitivities of portions of the mRNA for ribosomal protein S20 to 3'-exonucleases dependent on oligoadenylation and RNA secondary structure.Autoregulation allows Escherichia coli RNase E to adjust continuously its synthesis to that of its substrates
P2860
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P2860
RNase E activity is conferred by a single polypeptide: overexpression, purification, and properties of the ams/rne/hmp1 gene product
description
1993 nî lūn-bûn
@nan
1993 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
RNase E activity is conferred ...... the ams/rne/hmp1 gene product
@ast
RNase E activity is conferred ...... the ams/rne/hmp1 gene product
@en
RNase E activity is conferred ...... the ams/rne/hmp1 gene product
@nl
type
label
RNase E activity is conferred ...... the ams/rne/hmp1 gene product
@ast
RNase E activity is conferred ...... the ams/rne/hmp1 gene product
@en
RNase E activity is conferred ...... the ams/rne/hmp1 gene product
@nl
prefLabel
RNase E activity is conferred ...... the ams/rne/hmp1 gene product
@ast
RNase E activity is conferred ...... the ams/rne/hmp1 gene product
@en
RNase E activity is conferred ...... the ams/rne/hmp1 gene product
@nl
P2093
P2860
P356
P1476
RNase E activity is conferred ...... the ams/rne/hmp1 gene product
@en
P2093
G A Mackie
J L Genereaux
R S Cormack
P2860
P304
P356
10.1073/PNAS.90.19.9006
P407
P577
1993-10-01T00:00:00Z