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Journal of Bacteriology, February 2004, p. 1136-1146, Vol. 186, No. 4
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.4.1136-1146.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

The Bacillus subtilis Extracytoplasmic-Function ^X Factor Regulates Modification of the Cell Envelope and Resistance to Cationic Antimicrobial Peptides

Department of Microbiology, Cornell University, Ithaca, New York 14853-8101

Received 15 July 2003/ Accepted 12 September 2003

Bacillus subtilis contains seven extracytoplasmic-function factors that activate partially overlapping regulons. We here identify four additional members of the ^X regulon, pbpX (penicillin-binding protein), ywnJ, the dlt operon (D-alanylation of teichoic acids), and the pss ybfM psd operon (phosphatidylethanolamine biosynthesis). Modification of teichoic acids by esterification with D-alanine and incorporation of phosphatidylethanolamine into the cell membrane have a common consequence: in both cases positively charged amino groups are introduced into the cell envelope. The resulting reduction in the net negative charge of the cell envelope has been previously implicated as a resistance mechanism specific for cationic antimicrobial peptides. Consistent with this notion, we find that both sigX and dltA mutants are more sensitive to nisin than wild-type cells. We conclude that activation of the ^X regulon serves to alter cell surface properties to provide protection against antimicrobial peptides.

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