Cloning and Characterization of the Constitutively Expressed Chitinase C Gene from a Marine Bacterium, Salinivibrio costicola Strain 5SM-1

Journal of Bioscience and Bioengineering

Volumn 96, Issue 6, 2003, Pages 529-536

  Aunpad, Ratchaneewan ^a   Panbangred, Watanalai ^a  

^a MAHIDOL UNIVERSITY   (Thailand)

Author keywords

Chitinase; Cloning; Salinivibrio costicola; Site directed mutagenesis

Indexed keywords

AMINO ACIDS; BACTERIA; CATALYSIS; CLONING; CODES (SYMBOLS); ENZYMES; GENES; GLUCOSE; HYDROLYSIS;

OPEN READING FRAMES;

BIOMEDICAL ENGINEERING;

ASPARTIC ACID; CADHERIN; CHITIN DERIVATIVE; CHITINASE C; GLUCOSE; GLUTAMIC ACID; GLYCOSIDASE; SIGNAL PEPTIDE; UNCLASSIFIED DRUG;

AMINO ACID COMPOSITION; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIAL STRAIN; BACTERIOPLANKTON; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SUBSTRATE; ENZYME SYNTHESIS; GENE EXPRESSION; GENE REPRESSION; GENE STRUCTURE; GENETIC TRANSCRIPTION; MOLECULAR CLONING; MOLECULAR WEIGHT; MUTATION; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; OPERON; PROTEIN DOMAIN; SALINIVIBRIO COSTICOLA; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS;

BACTERIA (MICROORGANISMS); SALINIVIBRIO COSTICOLA; UNCULTURED MARINE BACTERIUM;

EID: 0345863800     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1263/jbb.96.529     Document Type: Article

References (34)

1. Gooday, G. W.: The ecology of chitin degradation, p. 387-430. In Marshall, K. C. (ed.), Advances in microbial ecology, vol. 11. Plenum Press, New York (1990).
2. Yu, C., Lee, A. M., Bassler, B. L., and Roseman, S.: Chitin utilization by marine bacteria. A physiological function for bacterial adhesion to immobilized carbohydrate. J. Biol. Chem., 266, 24260-24267 (1991).
3. Kupiec, R. C. and Chet, I.: The molecular biology of chitin digestion. Curr. Opin. Biotechnol., 9, 270-277 (1998).
4. Suginta, W., Robertson, P. A. W., Austin, B., Fry, S. C., and Fothergill-Gilmore, L. A.: Chitinases from Vibrio: activity screening and purification of ChiA from Vibrio carchariae. J. Appl. Microbiol., 89, 76-84 (2000).
5. Henrissat, B. and Bairoch, A.: New families in the classification of glycosyl hydrolases based on amino acid sequence similiarities. Biochem. J., 293, 781-788 (1993).
6. Techkarnjanaruk, S. and Goodman, A. E.: Multiple genes involved in chitin degradation from the marine bacterium Pseudoalteromonas sp. strain S91. Microbiology, 145, 925-934 (1999).
7. Tsujibo, H., Orikoshi, H., Tanno, H., Fujimoto, K., Miyamoto, K., Imada, C., Okami, Y., and Inamori, Y.: Cloning, sequence, and expression of a chitinase gene from a marine bacterium, Alteromonas sp. strain O-7. J. Bacteriol., 175, 176-181 (1993).
8. Morimoto, K., Karita, S., Kimura, T., Sakka, K., and Ohmiya, K.: Cloning, sequencing and expression of the gene encoding Clostridium paraputrificum chitinase chiB and analysis of the functions of novel cadherin-like domains and a chitin-binding domain. J. Bacteriol., 179, 7306-7314 (1997).
9. Watanabe, T., Suzuki, K., Oyahagi, W., Ohnishi, K., and Tanaka, H.: Gene cloning of chitinase A1 from Bacillus circulans WL-12 revealed its evolutionary relationship to Serratia chitinase and to the type 111 homology units of fibronectin. J. Biol. Chem., 265, 15659-15665 (1990).
10. Watanabe, T., Kobori, K., Miyashita, K., Fujii, T., Sakai, H., Uchida, M., and Tanaka, H.: Identification of glutamic acid 204 and aspartic 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity. J. Biol. Chem., 268, 18567-18572 (1993).
11. Laemmli, U. K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
12. Trudel, J. and Asselin, A.: Detection of chitinase activity after polyacrylamide gel electrophoresis. Anal. Biochem., 178, 362-366 (1989).
13. McGrew, R. B. and Green, M. D.: Enhanced removal of detergent and recovery of enzymatic activity following sodium dodecyl sulfate polyacrylamide gel electrophoresis: use of casein in gel wash buffer. Anal. Biochem., 189, 68-74 (1990).
14. Reissig, J. L., Strominer, J. L., and Leloi, L. F.: A modification colorimetric method for the estimation of N-acetylamino sugars. J. Biol. Chem., 27, 959-966 (1955).
15. Whistler, R. S. and BeMiller, J. N.: Chitin. J. Org. Chem., 27, 1161-1163 (1962).
16. Bradford, M. M.: A rapid and sensitive method for the quantitation of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
17. Ho, S. N., Hunt, H. D., Morton, R. M., Pullen, J. K., and Pease, L. R.: Site directed mutagenesis by overlap extension using the polymerase chain reaction. Gene, 77, 51-59 (1989).
18. Lee, H. S., Han, D. S., Choi, S. J., Choi, S. W., Kim, D. S., Bai, D. H., and Yu, J. H.: Purification, characterization, and primary structure of a chitinase from Pseudomonas sp. YHS-A2. Appl. Microbiol. Biotechnol., 54, 397-405 (2000).
19. Morimoto, K., Karita, S., Kimura, T., Sakka, K., and Ohmiya, K.: Sequencing, expression, and transcription analysis of the Clostridium paratrificum chiA gene encoding chitinase ChiA. Appl. Microbiol. Biotechnol., 51, 340-347 (1999).
20. 2+ binding site of uvomorulin abolish the adhesive function. Cell, 63, 1033-1038 (1990).
21. Tsujibo, H., Orikoshi, H., Baba, N., Miyahara, M., Miyamoto, K., Yasuda, M., and Inamori, Y.: Identification and characterization of the gene cluster involved in chitin degradation in a marine bacterium, Alteromonas sp. strain O-7. Appl. Environ. Microbiol., 68, 263-270 (2002).
22. Svitil, A. L. and Kirchman, D. L.: A chitin-binding domain in a marine bacterial chitinase and other microbial chitinases: implications for the ecology and evolution of 1,4-β-glycanase. Microbiology, 144, 1299-1308 (1998).
23. Tsujibo, H., Kondo, N., Tanaka, K., Miyamoto, K., Baba, N., and Inamori, Y.: Molecular analysis of the gene encoding a novel transglycosylative enzyme from Alteromonas sp. strain O-7 and its physiological role in the chitinolytic system. J. Bacteriol., 181, 5461-5466 (1999).
24. Thamthiankul, S., Suan-Ngay, S., Tantimavanich, S., and Panbangred, W.: Chitinase from Bacillus thuringiensis subsp. pakistani. Appl. Microbiol. Biotechnol., 56, 395-401 (2001).
25. Monreal, J. and Reese, E. T.: The chitinase of Serratia marcescens. Can. J. Microbiol., 15, 689-696 (1969).
26. Fujii, T. and Miyashita, K.: Multiple domain structure in a chitinase gene (chiC) of Streptomyces lividans. J. Gen. Microbiol., 139, 677-686 (1993).
27. Techkarnjanaruk, S., Pongpattanakitshote, S., and Goodman, A. E.: Use of promoterless lacZ gene insertion to investigate chitinase gene expression in the marine bacterium Pseudoalteromonas sp. strain S91. Appl. Environ. Microbiol., 63, 2989-2996 (1997).
28. Gupta, R., Saxena, R. K., Chaturvedi, P., and Virdi, J. S.: Chitinase production by Streptomyces viridificans. J. Appl. Bacteriol., 78, 378-383 (1995).
29. Watanabe, T., Kimura, K., Sumiya, T., Nikaidou, N., Suzuki, K., Suzuki, M., Taiyoji, M., Ferrer, S., and Regue, M.: Genetic analysis of the chitinase system of Serratia marcescens 2170. J. Bacteriol., 179, 7111-7117 (1997).
30. Thomas, C. J., Gooday, G. W., King, L. A., and Possee, R. D.: Mutagenesis of the active site coding region of the Autographa californica nucleopolyhedrovirus chiA gene. J. Gen. Virol., 8, 1403-1411 (2000).
31. Perrakis, A., Tews, I., Dauter, Z., Oppenheim, A. B., Chet, I., Wilson, K. S., and Vorgias, C. E.: Crystal structure of a bacterial chitinase at 2.3 Å resolution. Structure, 2, 1169-1180 (1994).
32. Uchiyama, T., Katouno, F., Nikaidou, N., Nonaka, T., Sugiyama, J., and Watanabe, T.: Roles of the exposed aromatic residues in crystalline chitin hydrolysis by chitinase A from Serratia marcescens 2170. J. Biol. Chem., 276, 41343-41349 (2001).
33. Lehninger, L. A., Nelson, L. D., and Lox, M. M.: Principles of biochemistry, 2nd ed., p. 943-944. Worth Publisher, NY, USA (1993).
34. Sitrit, Y., Vorgias, C. E., Chet, I., and Oppenheim, A. M.: Cloning and primary structure of the chiA gene from Aeromonas caviae. J. Bacteriol., 177, 4187-4189 (1995).