NDLI: PEPTIDE INHIBITOR OF CYTOKINESIS DURING SPORULATION IN BACILLUS SUBTILIS

Content Provider	PubMed Central
Author	Handler, Aaron A. Lim, Joo Eun Losick, Richard
Abstract	Cytokinesis in bacteria is mediated by the tubulin-like protein FtsZ, which forms a Z-ring at the division site. Using FtsZ as bait in a two-hybrid screen, we discovered a 40-amino acid peptide, termed MciZ, from Bacillus subtilis that appeared to interact with FtsZ. Cells engineered to produce MciZ during growth formed aseptate filaments that lacked Z-rings. A mutant resistant to the toxic effects of MciZ during growth harbored an amino-acid substitution near the GTP binding pocket of FtsZ. Synthetic MciZ inhibited the GTPase activity of FtsZ and its ability to polymerize. MciZ was produced during sporulation under the control of the transcription factor σE. In the absence of MciZ, the mother-cell compartment of the sporangium aberrantly formed a Z-ring at a time in development when cytokinetic events normally have ceased. We conclude that MciZ is a previously unrecognized inhibitor of FtsZ that prevents inappropriate Z-ring formation during sporulation. MciZ showed little sequence similarity to other peptides in the databases, except the mouse antimicrobial peptide CRAMP, which we speculate works in part by inhibiting cytokinesis.
Related Links	http://dx.doi.org/10.1111/j.1365-2958.2008.06173.x
Ending Page	599
Page Count	12
Starting Page	588
File Format	PDF
ISSN	0950382X
e-ISSN	13652958
Journal	Molecular microbiology
Issue Number	3
Volume Number	68
Language	English
Publisher Date	2008-05-01
Access Restriction	Open
Subject Keyword	Molecular Biology Microbiology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Microbiology

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