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Function of heterologous and truncated RNase P proteins in Bacillus subtilis
Author(s) -
Gößringer Markus,
Hartmann Roland K.
Publication year - 2007
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2007.05962.x
Subject(s) - biology , bacillus subtilis , rnase p , heterologous , function (biology) , computational biology , ribonuclease , ribonuclease iii , genetics , microbiology and biotechnology , rna , bacteria , gene , rna interference
Summary Bacterial RNase P is composed of an RNA subunit and a single protein (encoded by the rnpB and rnpA genes respectively). The Bacillus subtilis rnpA knockdown strain d7 was used to screen for functional conservation among bacterial RNase P proteins from a representative spectrum of bacterial subphyla. We demonstrate conserved function of bacterial RNase P (RnpA) proteins despite low sequence conservation. Even rnpA genes from psychrophilic and thermophilic bacteria rescued growth of B. subtilis d7 bacteria; likewise, terminal extensions and insertions between β strands 2 and 3, in the so‐called metal binding loop, were compatible with RnpA function in B. subtilis . A deletion analysis of B. subtilis RnpA defined the structural elements essential for bacterial RNase P function in vivo . We further extended our complementation analysis in B. subtilis strain d7 to the four individual RNase P protein subunits from three different Archaea, as well as to human Rpp21 and Rpp29 as representatives of eukaryal RNase P. None of these non‐bacterial RNase P proteins showed any evidence of being able to replace the B. subtilis RNase P protein in vivo , supporting the notion that archaeal/eukaryal RNase P proteins are evolutionary unrelated to the bacterial RnpA protein.