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Lookup NU author(s): Professor Rick Lewis
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© 2016 The Authors. Peptidoglycan (PG), an essential stress-bearing component of the bacterial cell wall, is synthesised by penicillin binding proteins (PBPs). PG synthesis at the cell division septum is necessary for constructing new poles of progeny cells, and cells cannot elongate without inserting new PG in the side-wall. The cell division regulator GpsB appears to coordinate PG synthesis at the septum during division and at the side-wall during elongation in rod-shaped and ovococcoid Gram-positive bacteria. How the control over PG synthesis is exerted is unknown. In this issue of Molecular Microbiology, Rued et al. show that in pneumococci GpsB forms complexes with PBP2a and PBP2b, and that deletion or depletion of GpsB prevents closure of the septal ring that in itself is PBP2x-dependent. Loss of GpsB can be suppressed by spontaneous mutations, including within the gene encoding the only PP2C Ser/Thr phosphatase in Streptococcus pneumoniae, indicating that GpsB plays a key – but unknown – role in protein phosphorylation in pneumococci. Rued et al. combine phenotypic and genotypic analyses of mutant strains that suggest discrepancies in the literature concerning GpsB might have arisen from accumulation of unidentified suppressors, highlighting the importance and power of strain validation and whole genome sequencing in this context.
Author(s): Lewis RJ
Publication type: Article
Publication status: Published
Journal: Molecular Microbiology
Print publication date: 01/03/2017
Online publication date: 23/12/2016
Acceptance date: 02/04/2016
ISSN (print): 0950-382X
ISSN (electronic): 1365-2958
Publisher: John Wiley & Sons Ltd
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