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 ...
Patricia Bralley +4 more
semanticscholar +5 more sources
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
semanticscholar +7 more sources
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
semanticscholar +6 more sources
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
semanticscholar +5 more sources
Crystal structure of the phosphorolytic exoribonuclease RNase PH from Bacillus subtilis and implications for its quaternary structure and tRNA binding [PDF]
Protein Science, 2004 AbstractRNase PH is a member of the family of phosphorolytic 3′ → 5′ exoribonucleases that also includes polynucleotide phosphorylase (PNPase). RNase PH is involved in the maturation of tRNA precursors and especially important for removal of nucleotide residues near the CCA acceptor end of the mature tRNAs.
Lene S. Harlow +3 more
semanticscholar +5 more sources
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
semanticscholar +5 more sources
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
semanticscholar +5 more sources
Identification of the rph (RNase PH) gene of Bacillus subtilis: evidence for suppression of cold-sensitive mutations in Escherichia coli [PDF]
Journal of Bacteriology, 1992 A shotgun cloning of Bacillus subtilis DNA into pBR322 yielded a 2-kb fragment that suppresses the cold-sensitive defect of the nusA10(Cs) Escherichia coli mutant. The responsible gene encodes an open reading frame that is greater than 50% identical at the amino acid level to the E. coli rph gene, which was formerly called orfE. This B.
M G Craven +6 more
semanticscholar +5 more sources
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
semanticscholar +5 more sources
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
semanticscholar +4 more sources