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 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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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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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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Crystal Structure of the tRNA Processing Enzyme RNase PH from Aquifex aeolicus [PDF]
Journal of Biological Chemistry, 2003 RNase PH is one of the exoribonucleases that catalyze the 3' end processing of tRNA in bacteria. RNase PH removes nucleotides following the CCA sequence of tRNA precursors by phosphorolysis and generates mature tRNAs with amino acid acceptor activity. In this study, we determined the crystal structure of Aquifex aeolicus RNase PH bound with a phosphate,
Ryohei Ishii +2 more
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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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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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RNase PH: an Escherichia coli phosphate-dependent nuclease distinct from polynucleotide phosphorylase. [PDF]
Proceedings of the National Academy of Sciences, 1988 Final trimming of the 3' terminus of tRNA precursors in Escherichia coli is thought to proceed by an exonucleolytic mechanism. However, mutant strains lacking as many as four exoribonucleases known to act on tRNA still grow normally and process tRNA normally.
Murray P. Deutscher +2 more
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Structural Basis of 3′ End RNA Recognition and Exoribonucleolytic Cleavage by an Exosome RNase PH Core [PDF]
Molecular Cell, 2005 The exosome is a macromolecular complex that plays fundamental roles in the biogenesis and turnover of a large number of RNA species. Here we report the crystal structures of the Rrp41-Rrp42 core complex of the S. solfataricus exosome bound to short single-stranded RNAs and to ADP.
Esben Lorentzen, Elena Conti
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