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Journal of Bacteriology, March 2009, p. 1556-1564, Vol. 191, No. 5
0021-9193/09/$08.00+0 doi:10.1128/JB.01493-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.
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Laboratoire de Chimie Bactérienne, UPR 9043, Institut de Biologie Structurale et Microbiologie, CNRS, 31 chemin Joseph Aiguier, 13402 Marseille Cedex 20, France
Received 23 October 2008/ Accepted 5 December 2008
The uncharacterized protein family UPF0042 of the Swiss-Prot database is predicted to be a member of the conserved group of bacterium-specific P-loop-containing proteins. Here we show that two of its members, YvcJ from Bacillus subtilis and YhbJ, its homologue from Escherichia coli, indeed bind and hydrolyze nucleotides. The cellular function of yvcJ was then addressed. In contrast to results recently obtained for E. coli, which indicated that yhbJ mutants strongly overproduced glucosamine-6-phosphate synthase (GlmS), comparison of the wild type with the yvcJ mutant of B. subtilis showed that GlmS expression was quite similar in the two strains. However, in mutants defective in yvcJ, the transformation efficiency and the fraction of cells that expressed competence were reduced. Furthermore, our data show that YvcJ positively controls the expression of late competence genes. The overexpression of comK or comS compensates for the decrease in competence of the yvcJ mutant. Our results show that even if YvcJ and YhbJ belong to the same family of P-loop-containing proteins, the deletion of corresponding genes has different consequences in B. subtilis and in E. coli.
Published ahead of print on 12 December 2008.
Supplemental material for this article may be found at http://jb.asm.org/.
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