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Control of the cell elongation–division cycle by shuttling of PBP1 protein in Bacillus subtilis
Author(s) -
Claessen Dennis,
Emmins Robyn,
Hamoen Leendert W.,
Daniel Richard A.,
Errington Jeff,
Edwards David H.
Publication year - 2008
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2008.06210.x
Subject(s) - cell division , bacillus subtilis , biology , microbiology and biotechnology , cell cycle , ftsz , elongation , penicillin binding proteins , division (mathematics) , cell , phenotype , cell cycle protein , cell growth , bacterial cell structure , cell wall , protein subcellular localization prediction , gene , genetics , bacterial protein , bacteria , materials science , arithmetic , mathematics , ultimate tensile strength , metallurgy
Summary The characteristic shape of bacterial cells is mainly determined by the cell wall, the synthesis of which is orchestrated by penicillin‐binding proteins (PBPs). Rod‐shaped bacteria have two distinct modes of cell wall synthesis, involved in cell elongation and cell division, which are believed to employ different sets of PBPs. A long‐held question has been how these different modes of growth are co‐ordinated in space and time. We have now identified the cell division protein, EzrA, and a newly discovered protein, GpsB, as key players in the elongation–division cycle of Bacillus subtilis . Mutations in these genes have a synthetic phenotype with defects in both cell division and cell elongation. They also have an unusual bulging phenotype apparently due to a failure in properly completing cell pole maturation. We show that these phenotypes are tightly associated with disturbed localization of the major transglycosylase/transpeptidase of the cell, PBP1. EzrA and GpsB have partially differentiated roles in the localization cycle of PBP1, with EzrA mainly promoting the recruitment of PBP1 to division sites, and GpsB facilitating its removal from the cell pole, after the completion of pole maturation.