In vitro binding of the CcpA protein of Bacillus megaterium to cis-acting catabolite responsive elements (CREs) of gram-positive bacteria.
Using DNA band migration retardation assays, specific binding of the CcpA protein of Bacillus megaterium to the cis-acting catabolite responsive element (CRE) of the xyl operon of B. subtilis has been demonstrated. Binding of CcpA was specifically inhibited by addition of unlabeled DNA fragments containing CREs of other operons but not by DNA fragments lacking a CRE. Binding was stimulated by high concentrations of phosphate, pyrophosphate, and organic phosphate esters and specifically inhibited by serine phosphorylated HPr and its conformational analogue, S46D HPr. This report therefore documents the specific binding of CcpA to a target CRE and defines its regulation by HPr(ser-P) and phosphorylated metabolites.
Ramseier
T M
TM
Department of Biology, University of California at San Diego, La Jolla 92093-0116, USA.
Reizer
J
J
Küster
E
E
Hillen
W
W
Saier
M H
MH
D001410:Bacillus megaterium / Q000378:metabolism*; D001426:Bacterial Proteins; D001483:Base Sequence; D001665:Binding Sites / Q000235:genetics; D002373:Cyclic AMP Receptor Protein / Q000235:genetics / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D006094:Gram-Positive Bacteria / Q000378:metabolism*; D008969:Molecular Sequence Data; D012097:Repressor Proteins / Q000378:metabolism*
D001426:Bacterial Proteins; D002373:Cyclic AMP Receptor Protein; D004268:DNA-Binding Proteins; D012097:Repressor Proteins; C069286:catabolite control proteins, bacteria