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J. Biol. Chem., Vol. 278, Issue 16, 14429-14441, April 18, 2003
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From the Division of Infectious Disease, Childrens Hospital and
Regional Medical Center, Seattle, Washington 98105
Protein phosphorylation is essential for the
regulation of cell growth, division, and differentiation in both
prokaryotes and eukaryotes. Signal transduction in prokaryotes was
previously thought to occur primarily by histidine kinases, involved in
two-component signaling pathways. Lately, bacterial homologues of
eukaryotic-type serine/threonine kinases and phosphatases have been
found to be necessary for cellular functions such as growth,
differentiation, pathogenicity, and secondary metabolism. The
Gram-positive bacteria Streptococcus agalactiae (group B
streptococci, GBS) is an important human pathogen. We have identified
and characterized a eukaryotic-type serine/threonine protein kinase
(Stk1) and its cognate phosphatase (Stp1) in GBS. Biochemical assays
revealed that Stk1 has kinase activity and localizes to the membrane
and that Stp1 is a soluble protein with manganese-dependent
phosphatase activity on Stk1. Mutations in these genes exhibited
pleiotropic effects on growth, virulence, and cell segregation of GBS.
Complementation of these mutations restored the wild type phenotype
linking these genes to the regulation of various cellular processes in
GBS. In vitro phosphorylation of cell extracts from wild
type and mutant strains revealed that Stk1 is essential for
phosphorylation of six GBS proteins. We have identified the
predominant endogenous substrate of both Stk1 and Stp1 as a
manganese-dependent inorganic pyrophosphatase (PpaC) by
liquid chromatography/tandem mass spectrometry. These results suggest
that these eukaryotic-type enzymes regulate pyrophosphatase activity
and other cellular functions of S. agalactiae.
A Eukaryotic Type Serine/Threonine Kinase and Phosphatase in
Streptococcus agalactiae Reversibly Phosphorylate an
Inorganic Pyrophosphatase and Affect Growth, Cell Segregation, and
Virulence*
*
This work was funded by Grant BWH 811501/NO1-AI-75326 from
the Streptococcal Initiative of the National Institutes of Health.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Pediatrics,
Div. of Infectious Disease, Mail Stop 8G-1, Children's Hospital and
Regional Medical Center, 4800 Sandpoint Way NE, Seattle, WA 98105. Tel.: 206-987-2073; Fax: 206-987-3890; E-mail:
craig.rubens@seattlechildrens.org.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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