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Characterization of TseB: A new actor in cell wall elongation in Bacillus subtilis
Author(s) -
Delisle Jordan,
Cordier Baptiste,
Audebert Stéphane,
Pophillat Matthieu,
Cluzel Caroline,
Espinosa Leon,
Grangeasse Christophe,
Galinier Anne,
Doan Thierry
Publication year - 2021
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.14798
Subject(s) - peptidoglycan , bacillus subtilis , penicillin binding proteins , biology , mutant , glycosyltransferase , cell wall , defensin , regulator , microbiology and biotechnology , biochemistry , gene , bacteria , escherichia coli , genetics
Penicillin‐binding proteins (PBPs) are crucial enzymes of peptidoglycan assembly and targets of β‐lactam antibiotics. However, little is known about their regulation. Recently, membrane proteins were shown to regulate the bifunctional transpeptidases/glycosyltransferases aPBPs in some bacteria. However, up to now, regulators of monofunctional transpeptidases bPBPs have yet to be revealed. Here, we propose that TseB could be such a PBP regulator. This membrane protein was previously found to suppress tetracycline sensitivity of a Bacillus subtilis strain deleted for ezrA , a gene encoding a regulator of septation ring formation. In this study, we show that TseB is required for B . subtilis normal cell shape, tseB mutant cells being shorter and wider than wild‐type cells. We observed that TseB interacts with PBP2A, a monofunctional transpeptidase. While TseB is not required for PBP2A activity, stability, and localization, we show that the overproduction of PBP2A is deleterious in the absence of TseB. In addition, we showed that TseB is necessary not only for efficient cell wall elongation during exponential phase but also during spore outgrowth, as it was also observed for PBP2A. Altogether, our results suggest that TseB is a new member of the elongasome that regulates PBP2A function during cell elongation and spore germination.