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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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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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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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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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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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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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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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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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
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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
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