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Originally published In Press as doi:10.1074/jbc.M200991200 on February 26, 2002

J. Biol. Chem., Vol. 277, Issue 19, 16606-16613, May 10, 2002
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The Aes Protein Directly Controls the Activity of MalT, the Central Transcriptional Activator of the Escherichia coli Maltose Regulon*

Nicolas JolyDagger §, Olivier DanotDagger , Anja Schlegel, Winfried Boos, and Evelyne RichetDagger ||

From the Dagger  Unité de Génétique Moléculaire, FRE CNRS 2364, Institut Pasteur, 25 rue de Dr. Roux, 75724 Paris Cedex 15, France and  Department of Biology, University of Konstanz, 78457 Konstanz, Germany

MalT, the transcriptional activator of the maltose regulon from Escherichia coli, is the prototype of a new family of transcription factors. Its activity is controlled by multiple regulatory signals. ATP and maltotriose (the inducer) are two effectors of the activator that positively control its multimerization, a critical step in promoter binding. In addition, MalK, the ABC component of the maltodextrin transport system, and the two enzymes MalY and Aes down-regulate MalT activity in vivo. By using a biochemical approach, we demonstrate here that (i) Aes controls MalT activity through direct protein-protein interaction, (ii) Aes competes with maltotriose for MalT binding, (iii) ATP and ADP differentially affect the competition between Aes and the inducer, and (iv) part, if not all, of the Aes binding site is located in DT1, the N-terminal domain of the activator, which also contains the ATP binding site. All of these characteristics point toward an identical mode of action for MalY and Aes. However, we have identified an amino acid substitution in MalT that suppresses MalT inhibition by Aes without interfering with its inhibition by MalY, suggesting that the binding sites of the two inhibitory proteins do not coincide. The differential effects of ATP and ADP on the competition between the inducer and Aes (or MalY) suggest that the ATPase activity displayed by MalT plays a role in the negative control of its activity.

* This work was supported in part by grants from the Deutsche Forschungsgemeinschaft and the Fonds der Chemischen Industrie.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported by the Ministère de la Recherche.

|| To whom correspondence should be addressed. Tel.: 33-1-40-61-36-80; Fax: 33-1-45-68-89-60; E-mail: erichet@pasteur.fr.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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