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J. Biol. Chem., Vol. 279, Issue 11, 9867-9874, March 12, 2004

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Cohesin-Dockerin Interactions within and between Clostridium josui and Clostridium thermocellum

BINDING SELECTIVITY BETWEEN COGNATE DOCKERIN AND COHESIN DOMAINS AND SPECIES SPECIFICITY^*

Sadanari Jindou, Akane Soda, Shuichi Karita, Tsutomu Kajino, Pierre Béguin¶, J. H. David Wu||, Minoru Inagaki, Tetsuya Kimura, Kazuo Sakka**, and Kunio Ohmiya

From the Faculty of Bioresources, Mie University, 1515 Kamihamacho, Tsu 514-8507, Japan, the Special Research Laboratory II, Toyota Central R&D Laboratories Inc., Nagakute, Aichi 480-1192, Japan, the ^¶Département des Biotechnologies, Institut Pasteur, 28, rue du Dr. Roux, 75724 Paris Cedex 15, France, and the ^||Department of Chemical Engineering, the University of Rochester, Rochester, New York 14627

The cellulosome components are assembled into the cellulosome complex by the interaction between one of the repeated cohesin domains of a scaffolding protein and the dockerin domain of an enzyme component. We prepared five recombinant cohesin polypeptides of the Clostridium thermocellum scaffolding protein CipA, two dockerin polypeptides of C. thermocellum Xyn11A and Xyn10C, four cohesin polypeptides of Clostridium josui CipA, and two dockerin polypeptides of C. josui Aga27A and Cel8A, and qualitatively and quantitatively examined the cohesin-dockerin interactions within C. thermocellum and C. josui, respectively, and the species specificity of the cohesin-dockerin interactions between these two bacteria. Surface plasmon resonance (SPR) analysis indicated that there was a certain selectivity, with a maximal 34-fold difference in the K_D values, in the cohesin-dockerin interactions within a combination of C. josui, although this was not detected by qualitative analysis. Affinity blotting analysis suggested that there was at least one exception to the species specificity in the cohesin-dockerin interactions, although species specificity was generally conserved among the cohesin and dockerin polypeptides from C. thermocellum and C. josui, i.e. the dockerin polypeptides of C. thermocellum Xyn11A exceptionally bound to the cohesin polypeptides from C. josui CipA. SPR analysis confirmed this exceptional binding. We discuss the relationship between the species specificity of the cohesin-dockerin binding and the conserved amino acid residues in the dockerin domains.

Received for publication, August 6, 2003 , and in revised form, December 9, 2003.

^* This work was supported in part by a Grant-in-aid for Scientific Research (A) (Grant 14206038) from the Ministry of Education, Culture, Sports, Science, and Technology, Japan. 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.

^** To whom correspondence should be addressed. Tel.: 81-59-231-9621; Fax: 81-59-231-9684; E-mail: sakka{at}bio.mie-u.ac.jp.

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