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S taphylococcus aureus DivIB is a peptidoglycan‐binding protein that is required for a morphological checkpoint in cell division
Author(s) -
Bottomley Amy L.,
Kabli Azhar F.,
Hurd Alexander F.,
Turner Robert D.,
GarciaLara Jorge,
Foster Simon J.
Publication year - 2014
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/mmi.12813
Subject(s) - biology , peptidoglycan , cell division , microbiology and biotechnology , cell cycle protein , cell , cell wall , genetics , cell cycle
Summary Bacterial cell division is a fundamental process that requires the coordinated actions of a number of proteins which form a complex macromolecular machine known as the divisome. The membrane‐spanning proteins DivIB and its orthologue FtsQ are crucial divisome components in G ram‐positive and G ram‐negative bacteria respectively. However, the role of almost all of the integral division proteins, including DivIB , still remains largely unknown. Here we show that the extracellular domain of DivIB is able to bind peptidoglycan and have mapped the binding to its β subdomain. Conditional mutational studies show that divIB is essential for S taphylococcus aureus growth, while phenotypic analyses following depletion of DivIB results in a block in the completion, but not initiation, of septum formation. Localisation studies suggest that DivIB only transiently localises to the division site and may mark previous sites of septation. We propose that DivIB is required for a molecular checkpoint during division to ensure the correct assembly of the divisome at midcell and to prevent hydrolytic growth of the cell in the absence of a completed septum.