JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Jiang, M.
Right arrow Articles by Perego, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jiang, M.
Right arrow Articles by Perego, M.

 Previous Article  |  Next Article 

Journal of Bacteriology, January 2000, p. 303-310, Vol. 182, No. 2
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Differential Processing of Propeptide Inhibitors of Rap Phosphatases in Bacillus subtilisdagger

Min Jiang,Dagger Roberto Grau,§ and Marta Perego*

The Scripps Research Institute, Department of Molecular and Experimental Medicine, Division of Cellular Biology, La Jolla, California 92037

Received 10 September 1999/Accepted 26 October 1999

In the phosphorelay signal transduction system for sporulation initiation in Bacillus subtilis, the opposing activities of histidine kinases and aspartyl phosphate phosphatases determine the cell's decision whether to continue with vegetative growth or to initiate the differentiation process. Regulated dephosphorylation of the Spo0A and Spo0F response regulators allows a variety of negative signals from physiological processes that are antithetical to sporulation to impact on the activation level of the phosphorelay. Spo0F~P is the known target of two related phosphatases, RapA and RapB. In addition to RapA and RapB, a third member of the Rap family of phosphatases, RapE, specifically dephosphorylated the Spo0F~P intermediate in response to competence development. RapE phosphatase activity was found to be controlled by a pentapeptide (SRNVT) generated from within the carboxy-terminal domain of the phrE gene product. A synthetic PhrE pentapeptide could (i) complement the sporulation deficiency caused by deregulated RapE activity of a phrE mutant and (ii) inhibit RapE-dependent dephosphorylation of Spo0F~P in in vitro experiments. The PhrE pentapeptide did not inhibit the phosphatase activity of RapA and RapB. These results confirm previous conclusions that the specificity for recognition of the target phosphatase is contained within the amino acid sequence of the pentapeptide inhibitor.

* Corresponding author. Mailing address: The Scripps Research Institute, Department of Molecular and Experimental Medicine, Division of Cellular Biology, 10550 N. Torrey Pines Rd., NX-1, La Jolla, CA 92037. Phone: 858-784-7912. Fax: 858-784-7966. E-mail: mperego{at}scripps.edu.

dagger Publication 12191-MEM of the Department of Molecular and Experimental Medicine, The Scripps Research Institute.

Dagger Present address: Stanford University, Palo Alto, CA 94305.

§ Present address: Facultad de Bioquimica y Farmacia, Departmento de Microbiologia, Promubie (CONICET), Rosario 2000, Argentina.

Journal of Bacteriology, January 2000, p. 303-310, Vol. 182, No. 2
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 2000 by the American Society for Microbiology. All rights reserved.