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Journal of Bacteriology, October 2009, p. 6020-6028, Vol. 191, No. 19
0021-9193/09/$08.00+0 doi:10.1128/JB.00605-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.
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Department of Microbiology, College of Physicians and Surgeons, Columbia University, New York, NY 10032
Received 8 May 2009/ Accepted 27 July 2009
Although peptidoglycan synthesis is one of the best-studied metabolic pathways in bacteria, the mechanism underlying the membrane translocation of lipid II, the undecaprenyl-disaccharide pentapeptide peptidoglycan precursor, remains mysterious. Recently, it was proposed that the essential Escherichia coli mviN gene encodes the lipid II flippase. Bacillus subtilis contains four proteins that are putatively homologous to MviN, including SpoVB, previously reported to be necessary for spore cortex peptidoglycan synthesis during sporulation. MviN complemented the sporulation defect of a
spoVB mutation, and SpoVB and another of the B. subtilis homologs, YtgP, complemented the growth defect of an E. coli strain depleted for MviN. Thus, these B. subtilis proteins are likely to be MviN homologs. However, B. subtilis strains lacking these four proteins have no defects in growth, indicating that they likely do not serve as lipid II flippases in this organism.
Published ahead of print on 7 August 2009.
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