RNA 3'-tail synthesis in Streptomyces: in vitro and in vivo activities of RNase PH, the SCO3896 gene product and polynucleotide phosphorylase

Microbiology
Patricia BralleyG H Jones

Abstract

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. First, it is confirmed that the product of S. coelicolor gene SCO3896, although it bears significant sequence similarity to Escherichia coli poly(A) polymerase I, is a tRNA nucleotidyltransferase, not a poly(A) polymerase. It is further shown that SCO2904 encodes an RNase PH homologue that possesses the polymerization and phosphorolysis activities expected for enzymes of that family. S. coelicolor RNase PH can add poly(A) tails to a model RNA transcript in vitro. However, disruption of the RNase PH gene has no effect on RNA 3'-tail length or composition in S. coelicolor; thus, RNase PH does not function as the RNA 3'-polyribonucleotide polymerase [poly(A) polymerase] in that organism. These results strongly suggest that the enzyme responsible for RNA 3'-tail synthesis in S. coelicolor and other streptomycetes is polynucleotide phosphorylase (PNPase). Moreover, this study shows that both PNPase and the product of SCO3896 are es...Continue Reading

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Citations

Jul 12, 2011·Journal of Bacteriology·Marcha L GatewoodGeorge H Jones
Sep 26, 2013·Cellular and Molecular Life Sciences : CMLS·Soumaya LaalamiHarald Putzer
Feb 24, 2011·Wiley Interdisciplinary Reviews. RNA·Bijoy K Mohanty, Sidney R Kushner
Oct 7, 2011·Wiley Interdisciplinary Reviews. RNA·Inês Jesus SilvaCecília Maria Arraiano
Apr 3, 2013·Biochimica Et Biophysica Acta·Cecília Maria ArraianoBertrand Séraphin
Jul 28, 2010·FEMS Microbiology Reviews·Cecília M ArraianoSandra C Viegas
Aug 23, 2019·Journal of Molecular Evolution·George H Jones
Nov 7, 2018·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·Eliane Hajnsdorf, Vladimir R Kaberdin

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