Characterization of dacC, which encodes a new low-molecular-weight penicillin-binding protein in Bacillus subtilis.

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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 sigmaH; 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 approximately 59-kDa membrane-associated penicillin-binding protein which is highly toxic when overexpressed.
Udgivelsesdato: 1998-Sep
Original languageEnglish
JournalJournal of Bacteriology
Volume180
Issue number18
Pages (from-to)4967-73
Number of pages6
ISSN0021-9193
Publication statusPublished - 1998

Bibliographical note

Keywords: Bacillus subtilis; Bacterial Proteins; Carrier Proteins; Escherichia coli; Genes, Bacterial; Hexosyltransferases; Lac Operon; Molecular Weight; Muramoylpentapeptide Carboxypeptidase; Mutation; Penicillin-Binding Proteins; Peptidyl Transferases; Transcription, Genetic

ID: 2830738