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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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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Effects of neutral salts and pH on the activity and stability of human RNase H2 [PDF]
The Journal of Biochemistry, 2017 Ribonuclease H (RNase H) specifically degrades the RNA of RNA/DNA hybrid. Recent study has shown that a single ribonucleotide is embedded in DNA double strand at every few thousand base pairs in human genome, and human RNase H2 is involved in its removal. Here, we examined the effects of neutral salts and pH on the activity and stability of human RNase
Misato Baba +7 more
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Characterization of Escherichia coli RNase PH.
Journal of Biological Chemistry, 1992 We have previously shown that the orfE gene of Escherichia coli encodes RNase PH. Here we show that the OrfE protein (purified as described in the accompanying paper) (Jensen, K. F., Andersen, J. T., and Poulsen, P. (1992) J. Biol. Chem. 267, 17147-17152) has both the degradative and synthetic activities of RNase PH.
K.O. Kelly, Murray P. Deutscher
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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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Overexpression and rapid purification of the orfE/rph gene product, RNase PH of Escherichia coli.
Journal of Biological Chemistry, 1992 The pyrE gene, encoding the pyrimidine biosynthetic enzyme orotate phosphoribosyltransferase, is the promoter distal gene of the dicistronic orfE-pyrE operon. The promoter proximal orfE gene, whose transcription and translation is important for regulation of the pyrE attenuator, encodes a 238-amino acid residue protein which was recently identified as ...
K.F. Jensen +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, 2010 Ribosomal RNAs are generally stable in growing Escherichia coli cells. However, their degradation increases dramatically under conditions that lead to slow cell growth. In addition, incomplete RNA molecules and molecules with defects in processing, folding, or assembly are also eliminated in growing cells in a process termed quality control.
Georgeta N. Basturea +2 more
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RNase PH is essential for tRNA processing and viability in RNase-deficient Escherichia coli cells.
Journal of Biological Chemistry, 1992 RNase PH is a Pi-dependent exoribonuclease that can act at the 3' terminus of tRNA precursors in vitro. To obtain information about the function of this enzyme in vivo, the Escherichia coli rph gene encoding RNase PH was interrupted with either a kanamycin resistance or a chloramphenicol resistance cassette and transferred to the chromosome of a ...
K.O. Kelly +3 more
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RNA 3′-tail synthesis in Streptomyces: in vitro and in vivo activities of RNase PH, the SCO3896 gene product and polynucleotide phosphorylase [PDF]
Microbiology, 2006 As in other bacteria, 3′-tails are added post-transcriptionally to Streptomyces coelicolor RNA. These tails are heteropolymeric, and although there are several candidates, the enzyme responsible for their synthesis has not been definitively identified. This paper reports on three candidates for this role.
Patricia Bralley +4 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 SummaryPolynucleotide phosphorylase (PNPase) catalyzes RNA polymerization and 3′→5′ phosphorolysis in vitro, but its roles in plant organelles are poorly understood. Here, we have used in vivo and in vitro mutagenesis to study Arabidopsis chloroplast PNPase (cpPNPase).
Arnaud Germain +5 more
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