NDLI: In Vivo Effects of Sporulation Kinases on Mutant Spo0A Proteins in Bacillus subtilis

Content Provider	PubMed Central
Author	Quisel, John D. Burkholder, William F. Grossman, Alan D.
Copyright Year	2001
Abstract	The phosphorylated form of the response regulator Spo0A (Spo0A∼P) is required for the initiation of sporulation in Bacillus subtilis. Phosphate is transferred to Spo0A from at least four histidine kinases (KinA, KinB, KinC, and KinD) by a phosphotransfer pathway composed of Spo0F and Spo0B. Several mutations in spo0A allow initiation of sporulation in the absence of spo0F and spo0B, but the mechanisms by which these mutations allow bypass of spo0F and spo0B are not fully understood. We measured the ability of KinA, KinB, and KinC to activate sporulation of five spo0A mutants in the absence of Spo0F and Spo0B. We also determined the effect of Spo0E, a Spo0A∼P-specific phosphatase, on sporulation of strains containing the spo0A mutations. Our results indicate that several of the mutations relax the specificity of Spo0A, allowing Spo0A to obtain phosphate from a broader group of phosphodonors. In the course of these experiments, we observed medium-dependent effects on the sporulation of different mutants. This led us to identify a small molecule, acetoin, that can stimulate sporulation of some spo0A mutants.
Related Links	http://dx.doi.org/10.1128/jb.183.22.6573-6578.2001
Ending Page	6578
Page Count	6
Starting Page	6573
File Format	PDF
ISSN	00219193
e-ISSN	10985530
Journal	Journal of Bacteriology
Issue Number	22
Volume Number	183
Language	English
Publisher	American Society for Microbiology
Publisher Date	2001-11-15
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Molecular Biology Microbiology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Microbiology

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