Phosphoprotein Crh-Ser46-P displays altered binding to CcpA to effect carbon catabolite regulation

doi:10.1074/jbc.M509977200

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Papers In Press, published online ahead of print November 29, 2005
J. Biol. Chem, 10.1074/jbc.M509977200
Submitted on September 12, 2005
Revised on November 18, 2005
Accepted on November 29, 2005

Phosphoprotein Crh-Ser46-P displays altered binding to CcpA to effect carbon catabolite regulation

Maria A. Schumacher, Gerald Seidel, Wolfgang Hillen, and Richard G. Brennan

Department of Biochemistry and Molecular Biology, University of Texas M.D. Anderson Cancer Center, Unit 1000, Houston, TX 77030

Corresponding Author: rgbrenna{at}mdanderson.org

In Gram positive bacteria, the Catabolite control protein A, (CcpA)³ functions as the master transcriptional regulator of carbon catabolite repression/regulation (CCR). To effect CCR, CcpA binds a phosphoprotein, either HPr-Ser46-P or Crh-Ser46-P. Although Crh and HPr are structurally homologous, CcpA binds Crh-Ser46-P more weakly than HPr-Ser46-P. Moreover, Crh can form domain-swapped dimers, which have been hypothesized to be functionally relevant in CCR. To understand the molecular mechanism of Crh-Ser46-P regulation of CCR, we determined the structure of a CcpA-(Crh-Ser46-P)-DNA complex. The structure reveals that Crh-Ser46-P does not bind CcpA as a dimer but rather interacts with CcpA as a monomer in a manner similar to that of HPr-Ser46-P. The reduced affinity of Crh-Ser46-P for CcpA as compared to that of HPr-Ser46-P is explained by weaker Crh-Ser46-P interactions in its Contact Region I to CcpA, which causes this region to shift away from CcpA. Nonetheless, the interface between CcpA and helix a2 of the second contact region (Contact Region II) of Crh-Ser46-P is maintained. This latter finding demonstrates that this contact region is necessary and sufficient to throw the allosteric switch to activate cre binding by CcpA.

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