Document Detail


Post-translational control of vegetative cell separation enzymes through a direct interaction with specific inhibitor IseA in Bacillus subtilis.
MedLine Citation:
PMID:  18761694     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Three D,L-endopeptidases, LytE, LytF and CwlS, are involved in the vegetative cell separation in Bacillus subtilis. A novel cell surface protein, IseA, inhibits the cell wall lytic activities of these d,l-endopeptidases in vitro, and IseA negatively regulates the cell separation enzymes at the post-translational level. Immunofluorescence microscopy indicated that the IseA-3xFLAG fusion protein was specifically localized at cell separation sites and poles on the vegetative cell surface in a similar manner of the d,l-endopeptidases. Furthermore, pull-down assay showed that IseA binds to the catalytic domain of LytF, indicating that IseA is localized on the cell surface through the catalytic domain of LytF. Overexpression of IseA caused a long-chained cell morphology in the exponential growth phase, indicating that IseA inhibits the cell separation D,L-endopeptidases in vivo. Besides, overexpression of IseA in a cwlO disruptant affected cell growth, implying that IseA is also involved in the cell elongation event. However, although IseA inhibits the activities of LytE, LytF, CwlS and CwlO in vitro, it is unlikely to inhibit CwlS and CwlO in vivo. This is the first demonstration that the cell separation event is post-translationally controlled through a direct interaction between cell separation enzymes and a specific novel inhibitor in bacteria.
Authors:
Hiroki Yamamoto; Masayuki Hashimoto; Yuhei Higashitsuji; Hiroyuki Harada; Nozomi Hariyama; Lisa Takahashi; Tomoaki Iwashita; Seika Ooiwa; Junichi Sekiguchi
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-08-27
Journal Detail:
Title:  Molecular microbiology     Volume:  70     ISSN:  1365-2958     ISO Abbreviation:  Mol. Microbiol.     Publication Date:  2008 Oct 
Date Detail:
Created Date:  2008-10-02     Completed Date:  2008-11-05     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8712028     Medline TA:  Mol Microbiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  168-82     Citation Subset:  IM    
Affiliation:
Experimental Farm, Faculty of Textile Science and Technology, Shinshu University, 3-15-1 Tokida, Ueda-shi, Nagano 386-8567, Japan.
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MeSH Terms
Descriptor/Qualifier:
Bacillus subtilis / enzymology*,  genetics,  growth & development
Bacterial Proteins / metabolism*
Carrier Proteins / metabolism*
Catalytic Domain
Cell Wall / enzymology*
DNA, Bacterial / genetics
Endopeptidases / metabolism*
Enzyme Inhibitors / metabolism
Genes, Bacterial
Membrane Proteins / metabolism
Microscopy, Fluorescence
Plasmids
Protein Processing, Post-Translational*
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Carrier Proteins; 0/DNA, Bacterial; 0/Enzyme Inhibitors; 0/Membrane Proteins; 0/yoeB protein, Bacillus subtilis; EC 3.4.-/Endopeptidases

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