Document Detail

YneA, an SOS-induced inhibitor of cell division in Bacillus subtilis, is regulated posttranslationally and requires the transmembrane region for activity.
MedLine Citation:
PMID:  20400548     Owner:  NLM     Status:  MEDLINE    
Cell viability depends on the stable transmission of genetic information to each successive generation. Therefore, in the event of intrinsic or extrinsic DNA damage, it is important that cell division be delayed until DNA repair has been completed. In Bacillus subtilis, this is accomplished in part by YneA, an inhibitor of division that is induced as part of the SOS response. We sought to gain insight into the mechanism by which YneA blocks cell division and the processes involved in shutting off YneA activity. Our data suggest that YneA is able to inhibit daughter cell separation as well as septum formation. YneA contains a LysM peptidoglycan binding domain and is predicted to be exported. We established that the YneA signal peptide is rapidly cleaved, resulting in secretion of YneA into the medium. Mutations within YneA affect both the rate of signal sequence cleavage and the activity of YneA. YneA does not stably associate with the cell wall and is rapidly degraded by extracellular proteases. Based on these results, we hypothesize that exported YneA is active prior to signal peptide cleavage and that proteolysis contributes to the inactivation of YneA. Finally, we identified mutations in the transmembrane segment of YneA that abolish the ability of YneA to inhibit cell division, while having little or no effect on YneA export or stability. These data suggest that protein-protein interactions mediated by the transmembrane region may be required for YneA activity.
Allison H Mo; William F Burkholder
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2010-04-16
Journal Detail:
Title:  Journal of bacteriology     Volume:  192     ISSN:  1098-5530     ISO Abbreviation:  J. Bacteriol.     Publication Date:  2010 Jun 
Date Detail:
Created Date:  2010-05-27     Completed Date:  2010-06-28     Revised Date:  2013-05-29    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3159-73     Citation Subset:  IM    
Department of Biology, Stanford University, 371 Serra Mall, Stanford, CA 94305-5020, USA.
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MeSH Terms
Amino Acid Sequence
Bacillus subtilis / genetics,  metabolism*
Bacterial Proteins / genetics,  metabolism*
Cell Division
Cytoskeletal Proteins / genetics,  metabolism
Gene Expression Regulation, Bacterial / physiology*
Models, Molecular
Molecular Sequence Data
Protein Processing, Post-Translational / physiology*
Son of Sevenless Proteins / genetics,  metabolism*
Grant Support
Reg. No./Substance:
0/Bacterial Proteins; 0/Cytoskeletal Proteins; 0/FtsZ protein, Bacteria; 0/Son of Sevenless Proteins

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