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Listeria monocytogenes EGD lacking penicillin-binding protein 5 (PBP5) produces a thicker cell wall

Lookup NU author(s): Professor Waldemar Vollmer

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Abstract

We report on the cloning of the structural gene for penicillin-binding protein 5 (PBP5), lmo2754. We also describe the enzymatic activity of PBP5 and characterize a mutant lacking this activity. Purified PBP5 has dd-carboxypeptidase activity, removing the terminal d-alanine residue from murein pentapeptide side chains. It shows higher activity against low molecular weight monomeric pentapeptide substrates compared to dimeric pentapeptide compound. Similarly, PBP5 preferentially cleaves monomeric pentapeptides present in high-molecular weight murein sacculi. A Listeria monocytogenes mutant lacking functional PBP5 was constructed. Cells of the mutant are viable, showing that the protein is dispensable for growth, but grow slower and have thickened cell walls.

Publication metadata

Author(s): Korsak D, Vollmer W, Markiewicz Z

Publication type: Article

Publication status: Published

Journal: FEMS Microbiology Letters

Year: 2005

Volume: 251

Issue: 2

Pages: 281-288

ISSN (print): 0378-1097

ISSN (electronic): 1574-6968

Publisher: Wiley-Blackwell Publishing Ltd.

URL: http://dx.doi.org/10.1016/j.femsle.2005.08.009

DOI: 10.1016/j.femsle.2005.08.009

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