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Microbiology 155 (2009), 3611-3621; DOI  10.1099/mic.0.030692-0
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Microbiology 155 (2009), 3611-3621; DOI  10.1099/mic.0.030692-0
© 2009 Society for General Microbiology

Influence of heterologous MreB proteins on cell morphology of Bacillus subtilis

Kathrin Schirner and Jeff Errington

Institute for Cell and Molecular Biosciences, Newcastle University, Medical School, Framlington Place, Newcastle Upon Tyne NE2 4HH, UK

The prokaryotic cytoskeletal protein MreB is thought to govern cell shape by positioning the cell wall synthetic apparatus at growth sites in the cell. In rod-shaped bacteria it forms helical filaments that run around the periphery of the rod during elongation. Gram-positive bacteria often contain more than one mreB gene. Bacillus subtilis has three mreB-like genes, mreB, mbl and mreBH, the first two of which have been shown to be essential under normal growth conditions. Expression of an mreB homologue from the closely related organism Bacillus licheniformis did not have any effect on cell growth or morphology. In contrast, expression of mreB from the phylogenetically more distant bacterium Clostridium perfringens produced shape defects and ultimately cell death, due to disruption of the endogenous MreB cytoskeleton. However, expression of either mreBB. licheniformis (mreBBl) or mreBC. perfringens (mreBCp) was sufficient to confer a rod shape to B. subtilis deleted for the three mreB isologues, supporting the idea that the three proteins have largely redundant functions in cell morphogenesis. Expression of mreBCDBl could fully compensate for the loss of mreBCD in B. subtilis and led to the formation of rod-shaped cells. In contrast, expression of mreBCDCp was not sufficient to confer a rod shape to B. subtilis {Delta}mreBCD, indicating that a complex of these three cell shape determinants is not enough for cell morphogenesis of B. subtilis.

Correspondence
Jeff Errington
jeff.errington{at}newcastle.ac.uk


Abbreviations: NA, nutrient agar; PAB, Difco Antibiotic Medium 3; YFP, yellow fluorescent protein







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