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Originally published In Press as doi:10.1074/jbc.M009237200 on January 8, 2001

J. Biol. Chem., Vol. 276, Issue 13, 9883-9888, March 30, 2001
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Cohesin-Dockerin Interaction in Cellulosome Assembly
A SINGLE HYDROXYL GROUP OF A DOCKERIN DOMAIN DISTINGUISHES BETWEEN NONRECOGNITION AND HIGH AFFINITY RECOGNITION*

Adva MechalyDagger , Henri-Pierre Fierobe§, Anne Belaich§, Jean-Pierre Belaich§, Raphael Lamed||, Yuval Shoham**, and Edward A. BayerDagger Dagger Dagger

From the Dagger  Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel, the § Bioénergétique et Ingéniérie des Protéines, Centre National de la Recherche Scientifique, IBSM-IFR1, Marseille 13402, France, the  Université de Provence, Marseille 13331, France, the || Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Ramat Aviv 69978, Israel, and the ** Department of Food Engineering and Biotechnology, and Institute of Catalysis Science and Technology, Technion-Israel Institute of Technology, Haifa 32000, Israel

The assembly of enzyme components into the cellulosome complex is dictated by the cohesin-dockerin interaction. In a recent article (Mechaly, A., Yaron, S., Lamed, R., Fierobe, H.-P., Belaich, A., Belaich, J.-P., Shoham, Y., and Bayer, E. A. (2000) Proteins 39, 170-177), we provided experimental evidence that four previously predicted dockerin residues play a decisive role in the specificity of this high affinity interaction, although additional residues were also implicated. In the present communication, we examine further the contributing factors for the recognition of a dockerin by a cohesin domain between the respective cellulosomal systems of Clostridium thermocellum and Clostridium cellulolyticum. In this context, the four confirmed residues were analyzed for their individual effect on selectivity. In addition, other dockerin residues were discerned that could conceivably contribute to the interaction, and the suspected residues were similarly modified by site-directed mutagenesis. The results indicate that mutation of a single residue from threonine to leucine at a given position of the C. thermocellum dockerin differentiates between its nonrecognition and high affinity recognition (Ka ~ 109 M-1) by a cohesin from C. cellulolyticum. This suggests that the presence or absence of a single decisive hydroxyl group is critical to the observed biorecognition. This study further implicates additional residues as secondary determinants in the specificity of interaction, because interconversion of selected residues reduced intraspecies self-recognition by at least three orders of magnitude. Nevertheless, as the latter mutageneses served to reduce but not annul the cohesin-dockerin interaction within this species, it follows that other subtle alterations play a comparatively minor role in the recognition between these two modules.

* This work was supported by a contract from the European Commission (Fourth Framework, Biotechnology Programme, BIO4-97-2303). Grants from the Israel Science Foundation (administered by the Israel Academy of Sciences and Humanities, Jerusalem) are gratefully acknowledged. Additional support was provided by the Otto Meyerhof Center for Biotechnology, established by the Minerva Foundation, (Munich, Germany).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.

Dagger Dagger To whom correspondence should be addressed: Tel.: 972-8-934-2373; Fax: 972-8-946-8256; E-mail: bfbayer@wicc.weizmann.ac.il.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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