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Appl Environ Microbiol, February 1998, p. 472-478, Vol. 64, No. 2
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Characterization of Chitinase C from a Marine Bacterium, Alteromonas sp. Strain O-7, and Its Corresponding Gene and Domain Structure

Hiroshi Tsujibo,1,* Hideyuki Orikoshi,1 Kayoko Shiotani,1 Miyuki Hayashi,1 Junko Umeda,1 Katsushiro Miyamoto,1 Chiaki Imada,2 Yoshiro Okami,2 and Yoshihiko Inamori1

Osaka University of Pharmaceutical Sciences, 4-20-1 Nasahara, Takatsuki, Osaka 569-11,1 and Institute of Microbial Chemistry, 3-14-23 Kamiosaki, Shinagawa, Tokyo 141,2 Japan

Received 11 August 1997/Accepted 19 November 1997

One of the chitinase genes of Alteromonas sp. strain O-7, the chitinase C-encoding gene (chiC), was cloned, and the nucleotide sequence was determined. An open reading frame coded for a protein of 430 amino acids with a predicted molecular mass of 46,680 Da. Alignment of the deduced amino acid sequence demonstrated that ChiC contained three functional domains, the N-terminal domain, a fibronectin type III-like domain, and a catalytic domain. The N-terminal domain (59 amino acids) was similar to that found in the C-terminal extension of ChiA (50 amino acids) of this strain and furthermore showed significant sequence homology to the regions found in several chitinases and cellulases. Thus, to evaluate the role of the domain, we constructed the hybrid gene that directs the synthesis of the fusion protein with glutathione S-transferase activity. Both the fusion protein and the N-terminal domain itself bound to chitin, indicating that the N-terminal domain of ChiC constitutes an independent chitin-binding domain.

* Corresponding author. Mailing address: Osaka University of Pharmaceutical Sciences, 4-20-1 Nasahara, Takatsuki, Osaka 569-11, Japan. Phone: (81-726) 90-1057. Fax: (81-726) 90-1057. E-mail: tsujibo{at}oysun01.oups.ac.jp.




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