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 ...
Sulthana S, Quesada E, Deutscher MP.
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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 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 Bowden KE +4 more
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Novel role for RNase PH in the degradation of structured RNA. [PDF]
J Bacteriol, 2012 Jain C.
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RNase PH: an Escherichia coli phosphate-dependent nuclease distinct from polynucleotide phosphorylase. [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 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 ...
Murray P. Deutscher +2 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
Ryohei Ishii +2 more
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Degradation of ribosomal RNA during starvation: Comparison to quality control during steady-state growth and a role for RNase PH [PDF]
RNA: A publication of the RNA Society, 2010 Ribosomal RNAs are generally stable in growing Escherichia coli cells. However, their degradation increases dramatically under conditions that lead to slow cell growth.
Georgeta N. Basturea +2 more
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Mutational analysis of Arabidopsis chloroplast polynucleotide phosphorylase reveals roles for both RNase PH core domains in polyadenylation, RNA 3′‐end maturation and intron degradation [PDF]
The Plant Journal, 2011 Polynucleotide phosphorylase (PNPase) catalyzes RNA polymerization and 3'→5' phosphorolysis in vitro, but its roles in plant organelles are poorly understood.
Arnaud Germain +5 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-Å crystal
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: A publication of the RNA Society, 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.
John R. Anderson +5 more
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