J. Bacteriol. doi:10.1128/JB.01181-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.
The yydFGHIJ operon of Bacillus subtilis encodes a peptide that induces the LiaRS two-component system
Bronwyn G. Butcher,
Yi-Pin Lin,
and
John D. Helmann*
Department of Microbiology, Cornell University, Ithaca, NY 14853
* To whom correspondence should be addressed. Email:
jdh9{at}cornell.edu.
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Abstract |
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The Bacillus subtilis LiaRS two-component system (TCS) responds to perturbations of the cell envelope induced by lipid II interacting antibiotics such as vancomycin, ramoplanin, nisin, and bacitracin. Here we characterize Tn7-generated mutations that induce the liaRS TCS. In addition to insertions in liaF, a known negative regulator of the LiaRS TCS, we identified two disruptions in the last two genes of the yydFGHIJ operon. This operon is predicted to encode a 49aa peptide (YydF), a modification enzyme (YydG), a membrane-embedded protease (YydH), and an ATP-binding cassette (ABC) transporter (YydIJ). Genome sequence comparisons suggest that the yydFGHIJ operon may have been acquired by horizontal transfer. Inactivation of the YydIJ transporter resulted in increased expression from the LiaR-dependent PliaI promoter only in the presence of the yydFGH genes. Cells harboring the complete yydFGHIJ operon induced LiaR activity in co-cultured cells lacking either this transporter or the complete operon. These results suggest that this operon is involved in the synthesis and export of a modified peptide (YydF*) that elicits cell envelope stress sensed by the LiaRS TCS.