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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 subtilis
Min
Jiang,
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.

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

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.
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