J. Bacteriol., 10 1996, 6001-6005, Vol 178, No. 20
Copyright © 1996, American Society for Microbiology

Identification and characterization of pbpC, the gene encoding Bacillus subtilis penicillin-binding protein 3

T Murray, DL Popham and P Setlow
Department of Biochemistry, University of Connecticut Health Center, Farmington 06030, USA.

Penicillin-binding proteins (PBPs) are enzymes involved in the synthesis of peptidoglycan structures in Bacillus subtilis such as the vegetative cell wall and the spore cortex. The B. subtilis sequencing project has identified a gene (orf16, EMBL accession number D38161) which exhibits significant sequence similarity to genes encoding class B high-molecular-weight PBPs. We have found that orf16 encodes PBP3 and have renamed this locus pbpC. Transcriptional fusions to lacZ were used to demonstrate that pbpC is transcribed primarily during log-phase growth, with lower amounts expressed during sporulation. During spore germination and outgrowth, pbpC expression resumes coincident with an increase in the optical density of the culture. The major promoter for pbpC is located just upstream of the gene; a low level of expression during sporulation appears to originate from much further upstream. Loss of PBP3 does not produce any detectable change in phenotype with respect to cell morphology, growth, sporulation, spore heat resistance, or spore germination and outgrowth. This was also true when the pbpC mutation was combined with mutations affecting other PBP-encoding genes to produce double mutants. These findings are consistent with previous evidence that many PBPs of B. subtilis have redundant functions within the cell.

This article has been cited by other articles:

• Scheffers, D.-J., Pinho, M. G. (2005). Bacterial Cell Wall Synthesis: New Insights from Localization Studies. Microbiol. Mol. Biol. Rev. 69: 585-607 [Abstract] [Full Text]  
• Scheffers, D.-J. (2005). Dynamic localization of penicillin-binding proteins during spore development in Bacillus subtilis. Microbiology 151: 999-1012 [Abstract] [Full Text]  
• Sapunaric, F., Franssen, C., Stefanic, P., Amoroso, A., Dardenne, O., Coyette, J. (2003). Redefining the Role of psr in {beta}-Lactam Resistance and Cell Autolysis of Enterococcus hirae. J. Bacteriol. 185: 5925-5935 [Abstract] [Full Text]  
• Wei, Y., Havasy, T., McPherson, D. C., Popham, D. L. (2003). Rod Shape Determination by the Bacillus subtilis Class B Penicillin-Binding Proteins Encoded by pbpA and pbpH. J. Bacteriol. 185: 4717-4726 [Abstract] [Full Text]  
• Rohrer, S., Berger-Bachi, B. (2003). FemABX Peptidyl Transferases: a Link between Branched-Chain Cell Wall Peptide Formation and {beta}-Lactam Resistance in Gram-Positive Cocci. Antimicrob. Agents Chemother. 47: 837-846 [Full Text]  
• Goffin, C., Ghuysen, J.-M. (2002). Biochemistry and Comparative Genomics of SxxK Superfamily Acyltransferases Offer a Clue to the Mycobacterial Paradox: Presence of Penicillin-Susceptible Target Proteins versus Lack of Efficiency of Penicillin as Therapeutic Agent. Microbiol. Mol. Biol. Rev. 66: 702-738 [Abstract] [Full Text]  
• Duez, C., Zorzi, W., Sapunaric, F., Amoroso, A., Thamm, I., Coyette, J. (2001). The penicillin resistance of Enterococcus faecalis JH2-2r results from an overproduction of the low-affinity penicillin-binding protein PBP4 and does not involve a psr-like gene. Microbiology 147: 2561-2569 [Abstract] [Full Text]  
• Tjalsma, H., Bolhuis, A., Jongbloed, J. D. H., Bron, S., van Dijl, J. M. (2000). Signal Peptide-Dependent Protein Transport in Bacillus subtilis: a Genome-Based Survey of the Secretome. Microbiol. Mol. Biol. Rev. 64: 515-547 [Abstract] [Full Text]  
• Murray, T., Popham, D. L., Pearson, C. B., Hand, A. R., Setlow, P. (1998). Analysis of Outgrowth of Bacillus subtilis Spores Lacking Penicillin-Binding Protein 2a. J. Bacteriol. 180: 6493-6502 [Abstract] [Full Text]  
• Murray, T., Popham, D. L., Setlow, P. (1998). Bacillus subtilis Cells Lacking Penicillin-Binding Protein 1 Require Increased Levels of Divalent Cations for Growth. J. Bacteriol. 180: 4555-4563 [Abstract] [Full Text]