title: Opposite allosteric mechanisms in TetR and CAP.
abstract: Regulation of the DNA binding affinity of an oligomeric protein can be considered to consist of an intrinsic component, in which the affinity of an individual DNA-binding domain is modulated in response to effector binding, and an extrinsic component, in which the relative position of the protein's two DNA-binding domains are altered so that they can or cannot contact both half-site operators simultaneously. We demonstrated directly that the TetR repressor utilizes an extrinsic mechanism and CAP, the catabolite activator protein, utilizes an intrinsic mechanism.
authors.affiliation: Department of Biophysics, Johns Hopkins University, Baltimore, Maryland 21218, USA.
authors.forename: Jennifer E
authors.initials: JE
authors.lastname: Seedorff
authors.forename: Michael E
authors.initials: ME
authors.lastname: Rodgers
authors.forename: Robert
authors.initials: R
authors.lastname: Schleif
mesh_terms: D000494:Allosteric Regulation; D000242:Cyclic AMP / Q000378:metabolism*; D002373:Cyclic AMP Receptor Protein / Q000737:chemistry / Q000378:metabolism*; D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D012097:Repressor Proteins / Q000737:chemistry / Q000378:metabolism*; D013752:Tetracycline / Q000378:metabolism*
chemical_list: D002373:Cyclic AMP Receptor Protein; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D012097:Repressor Proteins; C034811:tetracycline resistance-encoding transposon repressor protein; D004247:DNA; D000242:Cyclic AMP; D013752:Tetracycline