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(Received for publication, June, 25, 1997, and in revised form, August 1, 1997)
From the Catabolite repression of a number of catabolic
operons in bacilli is mediated by the catabolite control protein CcpA,
the phosphocarrier protein HPr from the
phosphoenolpyruvate-dependent sugar transport system (PTS),
and a cis-acting DNA sequence termed the
catabolite-responsive element (cre). We present evidence
that CcpA interacts with HPr that is phosphorylated at
Ser46 (Ser(P) HPr) and that these proteins form a specific
ternary complex with cre DNA. Titration experiments
following the circular dichroism signal of the cre DNA
indicate that this complex consists of two molecules of Ser(P) HPr, a
CcpA dimer, and the cre sequence. Limited proteolysis
experiments indicate that the domain structure of CcpA is similar to
other members of the LacI/GalR family of helix-turn-helix proteins,
comprised of a helix-turn-helix DNA domain and a C-terminal effector
domain. NMR titration of Ser(P) HPr demonstrates that the isolated
C-terminal domain of CcpA forms a specific complex with Ser(P) HPr but
not with unphosphorylated HPr. Based upon perturbations to the NMR
spectrum, we propose that the binding site of the C-terminal domain of
CcpA on Ser(P) HPr forms a contiguous surface that encompasses both
Ser(P)46 and His15, the site of phosphorylation
by enzyme I of the PTS. This allows CcpA to recognize the
phosphorylation state of HPr, effectively linking the process of sugar
import via the PTS to catabolite repression in bacilli.
Volume 272, Number 42,
Issue of October 17, 1997
pp. 26530-26535
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Binding of the Catabolite Repressor Protein CcpA to Its DNA
Target Is Regulated by Phosphorylation of its Corepressor HPr
,
University of Washington, Department of
Biochemistry and Biomolecular Structure Center, Seattle, Washington
98195-7742, the ¶ Lehrstuhl für Mikrobiologie, Institut
für Mikrobiologie, Biochemie und Genetik der Friedrich-Alexander
Universität Erlangen-Nürnberg, Staudstrasse 5, 91058 Erlangen, Germany, and the § Institut de Biologie et Chime
des Protéines, CNRS, 7 passage du Vercors, F-69367
Lyon Cedex 07, France
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