Open AccessMreB Drives De N ovo Rod Morphogenesis in Caulobacter crescentus via Remodeling of the Cell Wall
Author(s) -
Constantin N. Takacs,
Sebastián Poggio,
Godefroid Charbon,
Mathieu Pucheault,
Waldemar Vollmer,
Christine JacobsWagner
Publication year - 2010
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.01311-09
Subject(s) - mreb , caulobacter crescentus , peptidoglycan , biology , cytoskeleton , microbiology and biotechnology , lipid ii , penicillin binding proteins , morphogenesis , bacterial cell structure , actin , biophysics , biochemistry , cell , cell wall , bacteria , penicillin , genetics , antibiotics , cell cycle , gene
MreB, the bacterial actin-like cytoskeleton, is required for the rod morphology of many bacterial species. Disruption of MreB function results in loss of rod morphology and cell rounding. Here, we show that the widely used MreB inhibitor A22 causes MreB-independent growth inhibition that varies with the drug concentration, culture medium conditions, and bacterial species tested. MP265, an A22 structural analog, is less toxic than A22 for growth yet equally efficient for disrupting the MreB cytoskeleton. The action of A22 and MP265 is enhanced by basic pH of the culture medium. Using this knowledge and the rapid reversibility of drug action, we examined the restoration of rod shape in lemon-shapedCaulobacter crescentus cells pretreated with MP265 or A22 under nontoxic conditions. We found that reversible restoration of MreB function after drug removal causes extensive morphological changes including a remarkable cell thinning accompanied with elongation, cell branching, and shedding of outer membrane vesicles. We also thoroughly characterized the composition ofC. crescentus peptidoglycan by high-performance liquid chromatography and mass spectrometry and showed that MreB disruption and recovery of rod shape following restoration of MreB function are accompanied by considerable changes in composition. Our results provide insight into MreB function in peptidoglycan remodeling and rod shape morphogenesis and suggest that MreB promotes the transglycosylase activity of penicillin-binding proteins.