Cloning and characterization of the gene encoding endo-β-1,3-glucanase from Arthrobacter sp. NHB-10

Bioscience, Biotechnology and Biochemistry

Volumn 71, Issue 6, 2007, Pages 1568-1571

  Okazaki, Katsuichiro ^a   Nishimura, Naohito ^a   Matsuoka, Fumiyoshi ^a   Hayakawa, Shigeru ^a  

^a KAGAWA UNIVERSITY   (Japan)

Author keywords

Arthrobacter sp.; Endo 1,3 glucanase; Gene cloning

Indexed keywords

AMINO ACIDS; BACTERIA; CATALYSIS; CLONING; ENZYMES;

ARTHROBACTER SP.; GENE CLONING;

GENE ENCODING;

GLUCAN ENDO 1,3 BETA GLUCOSIDASE;

AMINO ACID SEQUENCE; ARTHROBACTER; ARTICLE; ENZYME ACTIVE SITE; ENZYMOLOGY; GENE STRUCTURE; GENETICS; MOLECULAR CLONING; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ARTHROBACTER; BASE SEQUENCE; CATALYTIC DOMAIN; CLONING, MOLECULAR; CONSERVED SEQUENCE; GENE COMPONENTS; GLUCAN ENDO-1,3-BETA-D-GLUCOSIDASE; MOLECULAR SEQUENCE DATA; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, NUCLEIC ACID;

ARTHROBACTER; ARTHROBACTER SP.; BACTERIA (MICROORGANISMS); STREPTOMYCES COELICOLOR;

EID: 34347341784     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70030     Document Type: Article

References (18)

1. Fleming, M., and Manners, D. J., A structural difference between the soluble and insoluble forms of laminarin. Biochem. J., 94, 17P (1965).
2. Jin, S.-Y., and Okazaki, K., Isolation of nigeran-degrading Arthrobacter sp. NHB-10 and properties of mycodextranase produced by the isolated bacterium. Seibutsu-kogaku Kaishi (in Japanese), 74, 23-27 (1996).
3. Coutinho, P. M., and Henrissat, B., Carbohydrate-Active Enzymes server at URT:http://afmb.cnrs-mrs.fr/~cazy/CAZY/index.html.
4. Okazaki, K., Kawabata, T., Nakano, M., and Hayakawa, S., Purification and properties of chitinase from Arthrobacter sp. NHB-10. Biosci. Biotechnol. Biochem., 63, 1644-1646 (1999).
5. Vazquenz-Garciduenas, S., Leal-Morales, C. A., and Herrera-Estrella, A., Analysis of β-1,3-glucanolytic system of the biocontrol agent Trichoderma harzianum. Appl. Environ. Microbiol., 64, 1442-1446 (1998).
6. Kawabata, T., Hayakawa, S., and Okazaki, K., Purification and properties of β-1,3-glucanase from Arthrobacter sp. NHB-10. Seibutsu-kogaku Kaishi (in Japanese), 77, 219-223 (1999).
7. Okazaki, K., Amano, T., Morimoto, T., Iemoto, T., Kawabata, T., Hayakawa, S., and Akimitsu, K., Cloning and nucleotide sequence of the mycodextranase gene from Streptomyces sp. J-13-3. Biosci. Biotechnol. Biochem., 65, 1684-1687 (2001).
8. Okazaki, K., Yamashita, Y., Noda, M., Sueyoshi, N., Kameshita, I., and Hayakawa, S., Molecular cloning and expression of the gene encoding family 19 chitinase from Streptomyces sp. J-13-3. Biosci. Biotechnol. Biochem., 68, 341-351 (2004).
9. Nikolskaya, A. N., Pitkin, J. W., Schaeffer, H. J., Ahn, J. H., and Walton, J. D., EXG1p, a novel exo-β1,3-glucanase from the fungus Cochliobolus carbonum, contains a repeated motif present in other proteins that interact with polysaccharides. Biochim. Biophys. Acta, 1425, 632-636 (1998).
10. Cohen-Kupiec, R., Broglie, K., Friesem, D., Broglie, R., and Chet, I., Molecular cloning and characterization of a novel β-1,3-exoglucanase related to mycoparasitism of Trichoderma harzianum. Gene, 226, 147-154 (1999).
11. Cruz, J., Pintor-Toro, J. A., Bentez, T., Llobell, A., and Romero, L. C., A novel end-β-1,3-glucanase, BGN13.1, involved in mycoparasitism of Trichoderma harzianum. J. Bacteriol., 177, 6937-6945 (1995).
12. Nobe, R., Sakakibara, Y., Ogawa, K., and Suiko, M., Cloning and expression of a novel Trichoderma viride laminarinase AI gene (lamAI). Biosci. Biotechnol. Biochem., 68, 2111-2119 (2004).
13. Kawai, R., Igarashi, K., and Samejima, M., Gene cloning and heterologous expression of glycoside hydrolase family 55 β-1,3-glucanase from the basidiomycete Phanerochaete chrysosporium. Biotechnol. Lett., 28, 365-371 (2006).
14. Rigden, D. J., and Franco, O. L., β-Helical catalytic domains in glycoside hydrolase families 49, 55 and 87: domain architecture, modeling and assignment of catalytic residues. FEBS Lett., 530, 225-232 (2002).
15. Bentley, S. D., Chater, K. F., Cerdeno-Tarraga, A. M., Challis, G. L., Thomson, N. R., James, K. D., Harris, D. E., Quail, M. A., Kieser, H., Harper, D., Bateman, A., Brown, S., Chandra, G., Chen, C. W., Collins, M., Cronin, A., Fraser, A., Goble, A., Hidalgo, J., Hornsby, T., Howarth, S., Huang, C. H., Kieser, T., Larke, L., Murphy, L., Oliver, K., O'Neil, S., Rabbinowitsch, E., Rajandream, M. A., Rutherford, K., Rutter, S., Seeger, K., Saunders, D., Sharp, S., Squares, R., Squares, S., Taylor, K., Warren, T., Wietzorrek, A., Woodward, J., Barrell, B. G., Parkhill, J., and Hopwood, D. A., Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2). Nature, 417, 141-147 (2002).
16. Ikeda, H., Ishikawa, J., Hanamoto, A., Shinose, M., Kikuchi, H., Shiba, T., Sakaki, Y., Hattori, M., and Omura, S., Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis. Nat. Biotechnol., 21, 526-531 (2003).
17. Yamashita, Y., and Okazaki, K, Purification and anti-fungal activity of recombinant chitinase from Escherichia coli carrying the family 19 chitinase gene of Streptomyces sp. J-13-3. Biosci. Biotechnol. Biochem., 68, 2193-2196 (2004).
18. Romanos, M., Advances in the use of Pichia pastoris for high-level gene expression. Curr. Opin. Biotechnol., 6, 527-533 (1995).