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J. Biol. Chem., Vol. 279, Issue 14, 14264-14272, April 2, 2004

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Evidence of an Intramolecular Interaction between the Two Domains of the BlaR1 Penicillin Receptor during the Signal Transduction^*

Sophie Hanique, Maria-Luigi Colombo, Erik Goormaghtigh¶||, Patrice Soumillion**, Jean-Marie Frère, and Bernard Joris

From the Centre d'Ingénierie des Protéines, Institut de Chimie, Université de Liège, B-4000 Sart-Tilman, ^¶Laboratory for the Structure and Function of Biological Membranes, Center for Structural Biology and Bioinformatics, Université Libre de Bruxelles, B-1050 Bruxelles, and ^**Institut des Sciences de la Vie, Laboratoire de Biochimie Physique et des Biopolymères, Université Catholique de Louvain, B-1348 Louvain-la-Neuve, Belgium

The BlaR1 protein is a penicillin-sensory transducer involved in the induction of the Bacillus licheniformis -lactamase. The amino-terminal domain of the protein exhibits four transmembrane segments (TM1-TM4) that form a four--helix bundle embedded in the plasma bilayer. The carboxyl-terminal domain of 250 amino acids (BlaR-CTD) fused at the carboxyl end of TM4 possesses the amino acid sequence signature of penicillin-binding proteins. This membrane topology suggests that BlaR-CTD and the BlaR-amino-terminal domain are responsible for signal reception and signal transduction, respectively. With the use of phage display experiments, we highlight herein an interaction between BlaR-CTD and the extracellular, 63-amino acid L2 loop connecting TM2 and TM3. This interaction does not occur in the presence of penicillin. This result suggests that binding of the antibiotic to BlaR1 might entail the release of the interaction between L2 and BlaR-CTD, causing a motion of the -helix bundle and transfer of the information to the cytoplasm of the cell. In addition, fluorescence spectroscopy, CD, and Fourier transform IR spectroscopy experiments indicate that in contrast to the behavior of the corresponding Staphylococcus aureus protein, the -lactam antibiotic does not induce a drastic conformational change in B. licheniformis BlaR-CTD.

Received for publication, December 10, 2003 , and in revised form, January 20, 2004.

^* This work was supported in part by the Belgian Program of Interuniversity Poles of Attraction (P5/33) and the Fonds de la Recherche Fondamentale et Collective, Brussels, Belgium (2.4530.03). 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.

Both authors contributed equally to this work. Fellows of the Fonds pour la Formation à la Recherche dans l'Industrie et l'Agriculture (Brussels, Belgium).

^|| Research Director, Fonds National de la Recherche Scientifique (Brussels, Belgium).

Research Associates, Fonds National de la Recherche Scientifique (Brussels, Belgium).

To whom correspondence should be addressed. Tel.: 0032-4-366-29-54; Fax: 0032-4-366-33-64; E-mail: bjoris{at}ulg.ac.be.

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