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Characterization of HMW-PBPs from the rod-shaped actinomycete Corynebacterium glutamicum: Peptidoglycan synthesis in cells lacking actin-like cytoskeletal structures

Lookup NU author(s): Dr Richard DanielORCiD

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Abstract

Analysis of the complete genome sequence of Corynebacterium glutamicum indicated that, in addition to ftsI, there are eight proteins with sequence motifs that are strongly conserved in penicillin binding proteins (PBPs): four genes that code for high-molecular-weight (HMW)-PBPs (PBP1a, PBP1b, PBP2a and PBP2b), two genes encoding low-molecular-weight PBPs (PBP4 and PBP4b) and two probable β-lactamases (PBP5 and PBP6). Here, the function of the four HMW-PBPs in C. glutamicum was investigated using a combination of genetic knockouts, enhanced green fluorescent protein 2 (EGFP2) fusions and penicillin staining of membrane preparations. The four HMW-PBPs were expressed in a growing culture of C. glutamicum, but none of four pbp genes was individually essential for the growth of the bacterium, and only the simultaneous disruption of both pbp1b and pbp2b was lethal. The fused EGFP2-PBP proteins were functional in vivo, which allowed correct determination of their cellular localization. EGFP2 fusions to PBP1a, PBP1b and PBP2b localized at the poles and at the septum, whereas EGFP2-PBP2a was predominantly found at the septum. Cefsulodin treatment specifically delocalized PBP1a and PBP1b (class A HMW-PBPs), whereas mecillinam caused the specific delocalization of PBP2b and PBP2a (class B HMW-PBPs). The results provide new insight into the mechanisms involved in the synthesis of the cell wall in this bacterial species, which lacks a known actin-like cytoskeletal structure. © 2007 The Authors.

Publication metadata

Author(s): Valbuena N, Letek M, Ordonez E, Ayala J, Daniel RA, Gil JA, Mateos LM

Publication type: Article

Publication status: Published

Journal: Molecular Microbiology

Year: 2007

Volume: 66

Issue: 3

Pages: 643-657

Print publication date: 01/11/2007

ISSN (print): 0950-382X

ISSN (electronic): 1365-2958

Publisher: Wiley-Blackwell

URL: http://dx.doi.org/10.1111/j.1365-2958.2007.05943.x

DOI: 10.1111/j.1365-2958.2007.05943.x

PubMed id: 17877698

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