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J Biol Chem, Vol. 274, Issue 50, 35950-35954, December 10, 1999
,
From the Department of Microbiology and Molecular Genetics, Harvard
Medical School, Boston, Massachusetts 02115
In Escherichia coli, changes in redox
condition of growth are sensed and signaled by the Arc two-component
system. This system consists of ArcB as the membrane-associated sensor
kinase and ArcA as the cytoplasmic response regulator. ArcB is a
tripartite kinase, possessing a primary transmitter, a receiver, and a
secondary transmitter domain that catalyzes the phosphorylation of ArcA via a His
Asp
His
Asp phosphorelay, as well as the
dephosphorylation of ArcA-P by a reverse phosphorelay. When ArcA and
ArcB were incubated with ATP, the peak levels of phosphorylated
proteins increased in the presence of the fermentation metabolites
D-lactate, acetate, or pyruvate. In this study, we report
that these effectors accelerate the autophosphorylation activity of
ArcB and enhance the transphosphorylation of ArcA, but have no effect
on the dephosphorylation of ArcA-P. Moreover, the presence of the
receiver domain of ArcB is essential for the effectors to influence the
autophosphorylation rate of the primary transmitter domain of ArcB.
Supported by Fellowship B-PD 11474-301 from the Swedish Natural
Science Research Council.
§
To whom correspondence should be addressed: Dept. of Microbiology
and Molecular Genetics, Harvard Medical School, 200 Longwood Ave.,
Boston, MA 02115. Tel.: 617-432-1925; Fax: 617-738-7664; E-mail:
elin@hms.harvard.edu.
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