Literature DB >> 29073018

Minimal and RNA-free RNase P in Aquifex aeolicus.

Astrid I Nickel1, Nadine B Wäber1, Markus Gößringer1, Marcus Lechner1, Uwe Linne2, Ursula Toth3, Walter Rossmanith3, Roland K Hartmann4.   

Abstract

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.

Entities:  

Keywords:  Aquifex aeolicus; HARP; protein-only RNase P; tRNA processing

Mesh:

Substances:

Year:  2017        PMID: 29073018      PMCID: PMC5651759          DOI: 10.1073/pnas.1707862114

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  39 in total

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