Inactivation of RNase P in Escherichia coli significantly changes post‐transcriptional RNA metabolism

In eucaryotes the 5'-terminal guanylate moiety of mature tRNAHis is added posttranscriptionally. To determine whether the same mechanism occurs in procaryotes, we processed in vitro-derived Escherichia coli tRNAHis precursors to mature tRNA, either in E. coli extracts or by using pure M1-RNA, the catalytic component of RNase P. The results show that the extra guanylate at the 5' end of mature E. coli tRNAHis is encoded in the gene and is found in tRNA as the result of an unusual cleavage by RNase P.

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Preparation of uniformly labeled NMR samples in Escherichia coli under the tight control of the araBAD promoter: expression of an archaeal homolog of the RNase P Rpp29 protein

Protein Expression and Purification ◽

10.1016/s1046-5928(02)00707-6 ◽

2003 ◽

Vol 28 (2) ◽

pp. 246-251 ◽

Cited By ~ 6

Author(s):

William P. Boomershine ◽

M.L. Stephen Raj ◽

Venkat Gopalan ◽

Mark P. Foster

Keyword(s):

Escherichia Coli ◽

Rnase P ◽

Tight Control

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Artificial regulation of gene expression in Escherichia coli by RNase P.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.92.24.11115 ◽

1995 ◽

Vol 92 (24) ◽

pp. 11115-11119 ◽

Cited By ~ 62

Author(s):

C. Guerrier-Takada ◽

Y. Li ◽

S. Altman

Keyword(s):

Gene Expression ◽

Escherichia Coli ◽

Regulation Of Gene Expression ◽

Rnase P ◽

Expression In Escherichia Coli

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Minimal and RNA-free RNase P in Aquifex aeolicus

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.1707862114 ◽

2017 ◽

Vol 114 (42) ◽

pp. 11121-11126 ◽

Cited By ~ 19

Author(s):

Astrid I. Nickel ◽

Nadine B. Wäber ◽

Markus Gößringer ◽

Marcus Lechner ◽

Uwe Linne ◽

...

Keyword(s):

Escherichia Coli ◽

Saccharomyces Cerevisiae ◽

Gene Transfer ◽

Horizontal Gene Transfer ◽

Rnase P ◽

Aquifex Aeolicus ◽

Trna Processing ◽

Hyperthermophilic Bacterium ◽

Domains Of Life

RNase P is an essential tRNA-processing enzyme in all domains of life. We identified an unknown type of protein-only RNase P in the hyperthermophilic bacterium Aquifex aeolicus: Without an RNA subunit and the smallest of its kind, the 23-kDa polypeptide comprises a metallonuclease domain only. The protein has RNase P activity in vitro and rescued the growth of Escherichia coli and Saccharomyces cerevisiae strains with inactivations of their more complex and larger endogenous ribonucleoprotein RNase P. Homologs of Aquifex RNase P (HARP) were identified in many Archaea and some Bacteria, of which all Archaea and most Bacteria also encode an RNA-based RNase P; activity of both RNase P forms from the same bacterium or archaeon could be verified in two selected cases. Bioinformatic analyses suggest that A. aeolicus and related Aquificaceae likely acquired HARP by horizontal gene transfer from an archaeon.

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