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J Biol Chem, Vol. 273, Issue 49, 32864-32869, December 4, 1998
From the Department of Microbiology and Molecular Genetics, Harvard
Medical School, Boston, Massachusetts 02115
Escherichia coli senses and signals
anoxic or low redox conditions in its growth environment by the Arc
two-component system. Under those conditions, the tripartite sensor
kinase ArcB undergoes autophosphorylation at the expense of ATP and
subsequently transphosphorylates its cognate response regulator ArcA
through a His 
Asp His Asp phosphorelay pathway. In this
study we used various combinations of wild-type and mutant ArcB domains
to analyze in vitro the pathway for signal decay. The
results indicate that ArcA-P dephosphorylation does not occur by direct
hydrolysis but by transfer of the phosphoryl group to the secondary
transmitter and subsequently to the receiver domain of ArcB. This
reverse phosphorelay involves both the conserved His-717 of the
secondary transmitter domain and the conserved Asp-576 of the receiver
domain of ArcB but not the conserved His-292 of its primary transmitter
domain. This novel pathway for signal decay may generally apply to
signal transduction systems with tripartite sensor kinases.
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