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J Biol Chem, Vol. 274, Issue 39, 27379-27384, September 24, 1999

The RdeA-RegA System, a Eukaryotic Phospho-relay Controlling cAMP Breakdown

Peter A. ThomasonDagger , David TraynorDagger , Jeffry B. Stock, and Robert R. KayDagger

From the Dagger  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

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.


Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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