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J Biol Chem, Vol. 274, Issue 39, 27379-27384, September 24, 1999
From the The regA and rdeA gene
products of Dictyostelium are involved in the regulation of
cAMP signaling. The response regulator, RegA, is composed of an
N-terminal receiver domain linked to a C-terminal
cAMP-phosphodiesterase domain. RdeA may be a phospho-transfer protein
that supplies phosphates to RegA. We show genetically that phospho-RegA
is the activated form of the enzyme in vivo, in that the
predicted site of aspartate phosphorylation is required for full
activity. We show biochemically that RdeA and RegA communicate, as
evidenced by phospho-transfer between the two proteins in
vitro. Phospho-transfer is dependent on the presumed
phospho-accepting amino acids, histidine 65 of RdeA and aspartate 212 of RegA, and occurs in both directions. Phosphorylation of RegA by a
heterologous phospho-donor protein activates RegA phosphodiesterase
activity at least 20-fold. Our results suggest that the histidine
phosphotransfer protein, RdeA, and the response regulator, RegA,
constitute two essential elements in a eukaryotic His-Asp phospho-relay
network that regulates Dictyostelium development and
fruiting body maturation.
The RdeA-RegA System, a Eukaryotic Phospho-relay Controlling cAMP
Breakdown
,,
Medical Research Council Laboratory of
Molecular Biology, Hills Road, Cambridge, CB2 2QH, United Kingdom
and the ¶ Department of Molecular Biology, Princeton University,
Princeton, New Jersey 08544
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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