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- Title
Post-translational control of vegetative cell separation enzymes through a direct interaction with specific inhibitor IseA in Bacillus subtilis.
- Authors
Yamamoto, Hiroki; Hashimoto, Masayuki; Higashitsuji, Yuhei; Harada, Hiroyuki; Hariyama, Nozomi; Takahashi, Lisa; Iwashita, Tomoaki; Ooiwa, Seika; Sekiguchi, Junichi
- Abstract
Threed,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 thesed,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 thed,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 separationd,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.
- Subjects
ENDOPEPTIDASES; CELL separation; BACILLUS subtilis; CELL membranes; BACTERIAL cell walls; IMMUNOFLUORESCENCE
- Publication
Molecular Microbiology, 2008, Vol 70, Issue 1, p168
- ISSN
0950-382X
- Publication type
Article
- DOI
10.1111/j.1365-2958.2008.06398.x