This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Google Scholar
Right arrow Articles by Vasudevan, P.
Right arrow Articles by Popham, D. L.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vasudevan, P.
Right arrow Articles by Popham, D. L.

 Previous Article  |  Next Article 

Journal of Bacteriology, October 2009, p. 6012-6019, Vol. 191, No. 19
0021-9193/09/$08.00+0     doi:10.1128/JB.00604-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Homologues of the Bacillus subtilis SpoVB Protein Are Involved in Cell Wall Metabolism {triangledown}

Pradeep Vasudevan, Jessica McElligott, Christa Attkisson, Michael Betteken, and David L. Popham*

Department of Biological Sciences, Virginia Tech, Blacksburg, Virginia 24061

Received 8 May 2009/ Accepted 24 July 2009

Members of the COG2244 protein family are integral membrane proteins involved in synthesis of a variety of extracellular polymers. In several cases, these proteins have been suggested to move lipid-linked oligomers across the membrane or, in the case of Escherichia coli MviN, to flip the lipid II peptidoglycan precursor. Bacillus subtilis SpoVB was the first member of this family implicated in peptidoglycan synthesis and is required for spore cortex polymerization. Three other COG2244 members with high similarity to SpoVB are encoded within the B. subtilis genome. Mutant strains lacking any or all of these genes (yabM, ykvU, and ytgP) in addition to spoVB are viable and produce apparently normal peptidoglycan, indicating that their function is not essential in B. subtilis. Phenotypic changes associated with loss of two of these genes suggest that they function in peptidoglycan synthesis. Mutants lacking YtgP produce long cells and chains of cells, suggesting a role in cell division. Mutants lacking YabM exhibit sensitivity to moenomycin, an antibiotic that blocks peptidoglycan polymerization by class A penicillin-binding proteins. This result suggests that YabM may function in a previously observed alternate pathway for peptidoglycan strand synthesis.

* Corresponding author. Mailing address: Department of Biological Sciences, Virginia Tech, Life Sciences I, MC0910, Washington St., Blacksburg, VA 24061. Phone: (540) 231-2529. Fax: (540) 231-4043. E-mail: dpopham{at}vt.edu

{triangledown} Published ahead of print on 31 July 2009.

Journal of Bacteriology, October 2009, p. 6012-6019, Vol. 191, No. 19
0021-9193/09/$08.00+0     doi:10.1128/JB.00604-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»