Characterization of Chitinase C from a Marine Bacterium, Alteromonas sp. Strain O-7, and Its Corresponding Gene and Domain Structure
| Autor: | Katsushiro Miyamoto, Yoshihiko Inamori, Junko Umeda, Kayoko Shiotani, Hideyuki Orikoshi, Chiaki Imada, Yoshiro Okami, Hiroshi Tsujibo, Miyuki Hayashi |
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| Rok vydání: | 1998 |
| Předmět: |
Recombinant Fusion Proteins
Molecular Sequence Data Sequence alignment Biology Applied Microbiology and Biotechnology Homology (biology) Amino Acid Sequence Enzymology and Protein Engineering Cloning Molecular Alteromonas Peptide sequence chemistry.chemical_classification Base Sequence Gram-Negative Aerobic Bacteria Ecology Chitinases Nucleic acid sequence biology.organism_classification Amino acid Open reading frame chemistry Biochemistry Chitinase biology.protein Food Science Biotechnology |
| Zdroj: | Applied and Environmental Microbiology. 64:472-478 |
| ISSN: | 1098-5336 0099-2240 |
| DOI: | 10.1128/aem.64.2.472-478.1998 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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