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(Received for publication, July 12, 1996)
From the Department of Microbiology and Immunology, School of
Medicine, and § Molecular Biology Institute, UCLA,
Los Angeles, California 90024
Two-component systems use
phosphorylation reactions to regulate stimulus/response pathways. In
Bordetella pertussis, a human respiratory pathogen, the
infectious cycle of the organism is controlled by the BvgAS
two-component system. BvgS has similarities to sensor and response
regulator components and is an autophosphorylating kinase that
phosphorylates BvgA. BvgA, a response regulator, is a DNA-binding
protein that activates virulence gene transcription. Three
phosphorylated BvgS domains, the transmitter, receiver, and C terminus,
are essential for signal transduction. We now demonstrate that the BvgS
transmitter is sufficient for autophosphorylation but is unable to
phosphorylate the C terminus or BvgA. The BvgS receiver regulates
several phenotypes: dephosphorylation of both the BvgS transmitter and
C terminus as well as transfer of a phosphoryl group from the
transmitter to the C terminus. Our results indicate that BvgAS signal
transduction initiates with autophosphorylation of the transmitter
followed by phosphotransfer to the receiver. The phosphorylated
receiver can donate to the C terminus or to water. The phosphorylated C
terminus is then able to transfer the phosphoryl group to BvgA.
Volume 271, Number 52,
Issue of December 27, 1996
pp. 33176-33180
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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