Journal
NUCLEIC ACIDS RESEARCH
Volume 45, Issue 12, Pages 7441-7454Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkx405
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Funding
- German Research Foundation (DFG) [HA 1672/17-1, IRTG 1384]
- Austrian Science Fund (FWF) [I299]
- Austrian Science Fund (FWF) [W1207] Funding Source: Austrian Science Fund (FWF)
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The RNase P family comprises structurally diverse endoribonucleases ranging from complex ribonucleoproteins to single polypeptides. We show that the organellar (AtPRORP1) and the two nuclear (AtPRORP2,3) single-polypeptide RNase P isoenzymes from Arabidopsis thaliana confer viability to Escherichia coli cells with a lethal knockdown of its endogenous RNA-based RNase P. RNA-Seq revealed that AtPRORP1, compared with bacterial RNase P or AtPRORP3, cleaves several precursor tRNAs (pre-tRNAs) aberrantly in E. coli. Aberrant cleavage by AtPRORP1 was mainly observed for pre-tRNAs that can form short acceptor-stem extensions involving G:C base pairs, including tRNA(Asp)(GUC), tRNA(Ser)(CGA) and tRNA(His). However, both AtPRORP1 and 3 were defective in processing of E. coli pre-tRNA(Sec) carrying an acceptor stem expanded by three G: C base pairs. Instead, pre-tRNA(Sec) was degraded, suggesting that tRNA(Sec) is dispensable for E. coli under laboratory conditions. AtPRORP1, 2 and 3 are also essentially unable to process the primary transcript of 4.5S RNA, a hairpin-like non-tRNA substrate processed by E. coli RNase P, indicating that PRORP enzymes have a narrower, more tRNA-centric substrate spectrum than bacterial RNA-based RNase P enzymes. The cells' viability also suggests that the essential function of the signal recognition particle can be maintained with a 5'-extended 4.5S RNA.
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