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Journal of Bacteriology, September 1998, p. 4967-4973, Vol. 180, No. 18
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Characterization of dacC, Which Encodes a New Low-Molecular-Weight Penicillin-Binding Protein in Bacillus subtilis

Lotte B. Pedersen,1 Thomas Murray,1 David L. Popham,2 and Peter Setlow1,*

Department of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 06032,1 and Department of Biology, Virginia Polytechnic Institute and State University, Blacksburg, Virginia 24061-04062

Received 27 April 1998/Accepted 15 July 1998

The pbp gene (renamed dacC), identified by the Bacillus subtilis genome sequencing project, encodes a putative 491-residue protein with sequence homology to low-molecular-weight penicillin-binding proteins. Use of a transcriptional dacC-lacZ fusion revealed that dacC expression (i) is initiated at the end of stationary phase; (ii) depends strongly on transcription factor sigma H; and (iii) appears to be initiated from a promoter located immediately upstream of yoxA, a gene of unknown function located upstream of dacC on the B. subtilis chromosome. A B. subtilis dacC insertional mutant grew and sporulated identically to wild-type cells, and dacC and wild-type spores had the same heat resistance, cortex structure, and germination and outgrowth kinetics. Expression of dacC in Escherichia coli showed that this gene encodes an ~59-kDa membrane-associated penicillin-binding protein which is highly toxic when overexpressed.

* Corresponding author. Mailing address: Department of Biochemistry, University of Connecticut Health Center, 263 Farmington Ave., Farmington, CT 06032. Phone: (860) 679-2607. Fax: (860) 679-3408. E-mail: setlow{at}sun.uchc.edu.

Journal of Bacteriology, September 1998, p. 4967-4973, Vol. 180, No. 18
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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