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Journal of Bacteriology, October 2005, p. 7146-7149, Vol. 187, No. 20
0021-9193/05/$08.00+0     doi:10.1128/JB.187.20.7146-7149.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Site-Directed Mutagenesis and Expression of the Soluble Form of the Family IIIa Cellulose Binding Domain from the Cellulosomal Scaffolding Protein of Clostridium cellulovorans

Koichiro Murashima, Akihiko Kosugi, and Roy H. Doi^*

Section of Molecular and Cellular Biology, University of California, Davis, California 95616

Received 22 April 2005/ Accepted 27 July 2005

The planar and anchoring residues of the family IIIa cellulose binding domain (CBD) from the cellulosomal scaffolding protein of Clostridium cellulovorans were investigated by site-directed mutagenesis and cellulose binding studies. By fusion with maltose binding protein, the family IIIa recombinant wild-type and mutant CBDs from C. cellulovorans were expressed as soluble forms. Cellulose binding tests of the mutant CBDs indicated that the planar strip residues played a major role in cellulose binding and that the anchoring residues played only a minor role.

Present address: Meiji Seika Kaisha, Ltd., Sakado-shi, Saitama 350-0289, Japan.

Present address: Japan International Research Center for Agricultural Sciences (JIRCAS), Tsukuba, Ibaraki 305-8686, Japan.

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