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Opposite allosteric mechanisms in TetR and CAP
Author(s) -
Seedorff Jennifer E.,
Rodgers Michael E.,
Schleif Robert
Publication year - 2009
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.88
Subject(s) - tetr , allosteric regulation , repressor , effector , catabolite repression , biophysics , activator (genetics) , dna , allosteric enzyme , chemistry , mechanism (biology) , microbiology and biotechnology , dna binding domain , binding site , lac repressor , biology , biochemistry , transcription factor , physics , receptor , gene , mutant , quantum mechanics
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.