Results 1 to 10 of about 315,883 (294)
RNase II regulates RNase PH and is essential for cell survival during starvation and stationary phase. [PDF]
RNA, 2017 RNase II is the most active exoribonuclease in Escherichia coli cell extracts. Yet, its removal appears to have no deleterious effect on growing cells. Here, we show that RNase II is required for cell survival during prolonged stationary phase and upon starvation.
Sulthana S, Quesada E, Deutscher MP.
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Novel role for RNase PH in the degradation of structured RNA. [PDF]
J Bacteriol, 2012 ABSTRACTEscherichia colicontains multiple 3′ to 5′ RNases, of which two, RNase PH and polynucleotide phosphorylase (PNPase), use inorganic phosphate as a nucleophile to catalyze RNA cleavage. It is known that an absence of these two enzymes causes growth defects, but the basis for these defects has remained undefined. To further an understanding of the
Jain C.
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The rph-1-Encoded Truncated RNase PH Protein Inhibits RNase P Maturation of Pre-tRNAs with Short Leader Sequences in the Absence of RppH. [PDF]
J Bacteriol, 2017 ABSTRACT RNase PH, encoded by the rph gene, is a 3′→5′ exoribonuclease that in E. coli participates primarily in the 3′ maturation of pre-tRNAs and the degradation of rRNA in stationary-phase cells.
Bowden KE +4 more
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The Phosphorolytic Exoribonucleases Polynucleotide Phosphorylase and RNase PH Stabilize sRNAs and Facilitate Regulation of Their mRNA Targets. [PDF]
J Bacteriol, 2016 ABSTRACT Gene regulation by base pairing between small noncoding RNAs (sRNAs) and their mRNA targets is an important mechanism that allows bacteria to maintain homeostasis and respond to dynamic environments. In Gram-negative bacteria, sRNA pairing and regulation are mediated by several RNA-binding proteins, including the sRNA ...
Cameron TA, De Lay NR.
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Escherichia coli orfE (upstream of pyrE) encodes RNase PH [PDF]
Journal of Bacteriology, 1991 RNase PH from extracts of Escherichia coli was purified to homogeneity and subjected to NH2-terminal sequencing. Comparison of this sequence with all open reading frames in the GenBank data base revealed at least 95% identity to an unidentified open reading frame (orfE) upstream of pyrE at 81.7 min on the E. coli chromosome.
K A Ost, Murray P. Deutscher
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Identification of the Acidification Mechanism of the Optimal pH for RNase He1
Biological and Pharmaceutical Bulletin, 2023 Ribonuclease (RNase) He1 is a small ribonuclease belonging to the RNase T1 family. Most of the RNase T1 family members are active at neutral pH, except for RNase Ms, U2, and He1, which function at an acidic pH. We crystallized and analyzed the structure of RNase He1 and elucidated how the acidic amino residues of the α1β3- (He1:26-33) and β67-loops ...
Katsuki Takebe +7 more
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Implication of RNases PH in Turnover of M1 RNA [PDF]
Bulletin of the Korean Chemical Society, 2010 Figure 1. Effects on sequestration of C5 protein on M1 RNA stability in endoribonuclease-deficient cells. Total cellular RNA was isolated from strains GW10 (wild type), GW11 (rng‒), and GW20 (rne) containing plasmids at the indicated times after the rifampicin treatment. Each RNA sample (30 μg) was fractionated on a 5% polyacrylamide gel containing 7 M
Yool Kim +4 more
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An essential function for the phosphate-dependent exoribonucleases RNase PH and polynucleotide phosphorylase [PDF]
Journal of Bacteriology, 1997 Escherichia coli cells lacking both polynucleotide phosphorylase (PNPase) and RNase PH, the only known P(i)-dependent exoribonucleases, were previously shown to grow slowly at 37 degrees C and to display a dramatically reduced level of tRNA(Tyr)su3+ suppressor activity. Here we show that the RNase PH-negative, PNP-negative double-mutant strain actually
Zheng Zhou, Murray P. Deutscher
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Probing the Functional Importance of the Hexameric Ring Structure of RNase PH [PDF]
Journal of Biological Chemistry, 2003 RNase PH is a phosphate-dependent exoribonuclease that catalyzes the removal of nucleotides at the 3' end of the tRNA precursor, leading to the release of nucleoside diphosphate, and generates the CCA end during the maturation process. The 1.9-A crystal structures of the apo and the phosphate-bound forms of RNase PH from Pseudomonas aeruginosa reveal a
Jung Min Choi +4 more
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Sequence-specific RNA binding mediated by the RNase PH domain of components of the exosome [PDF]
RNA, 2006 We have previously demonstrated that PM-Scl-75, a component of the human exosome complex involved in RNA maturation and mRNA decay, can specifically interact with RNAs containing an AU-rich instability element. Through the analysis of a series of deletion mutants, we have now shown that a 266 amino acid fragment representing the RNase PH domain is ...
John R. Anderson +5 more
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