ArticleOpposite allosteric mechanisms in TetR and CAP |
| Jennifer E. Seedorff 1, Michael E. Rodgers 2, Robert Schleif 2 * |
1Department of Biophysics, Johns Hopkins University, Baltimore, Maryland 21218
2Department of Biology, Johns Hopkins University, Baltimore, Maryland 21218
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| email: Robert Schleif (schleif@jhu.edu) |
*Correspondence to Robert Schleif, Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, Maryland 21218-2685
Funded by:
NIH; Grant Number: GM018277
| Tet Repressor CAP CRP allostery DNA-binding protein half-site operator extrinsic allosteric mechanism intrinsic allosteric mechanism |
| 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. |
Received: 30 October 2008; Revised: 22 January 2009; Accepted: 28 January 2009
10.1002/pro.88
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