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J. Biol. Chem., Vol. 280, Issue 26, 24591-24599, July 1, 2005
A Peptide Triggers Allostery in Tet Repressor by Binding to a Unique Site*![]() From the Lehrstuhl für Mikrobiologie, Institut für Mikrobiologie, Biochemie und Genetik, Friedrich-Alexander Universität Erlangen-Nürnberg, Staudtstrasse 5, 91058 Erlangen, Germany Regulatory proteins often communicate with each other to manage various cellular processes. Such interactions mostly rely on the recognition of small peptide motifs. The activity of other regulatory proteins depends on small molecular weight effectors and allostery. We demonstrate the in vivo regulation of the tetracycline-dependent Tet repressor by an oligopeptide fused to the N or C terminus of thioredoxin A. The binding site of the peptide overlaps but is not identical with the tetracycline binding site. Several TetR mutants that are non-inducible by tetracycline also respond to the peptide. This demonstrates for the first time the conversion of a small molecular weight effector-dependent regulator to a protein-protein contact-dependent potential member of designed signaling chains.
Received for publication, February 18, 2005 , and in revised form, May 2, 2005. * This work was supported by the Deutsche Forschungsgemeinschaft through the SFB 473, the Graduierten Kolleg 805, and the Fonds der Chemischen Industrie. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
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