Molecular characterization of the Thermomonospora curvata agIA gene encoding a thermotolerant α-1,4-glucosidase

Journal of Applied Microbiology

Volumn 88, Issue 5, 2000, Pages 773-783

  Janda, L ^a   Damborsky J ^b   Petricek M ^a   Spizek J ^a   Tichy P ^a  

^a INSTITUTE OF MICROBIOLOGY   (Czech Republic)

^b MASARYK UNIVERSITY   (Czech Republic)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASES; BACILLUS CEREUS; BACTERIOLOGY; COMPUTER AIDED ANALYSIS; ENCODING (SYMBOLS); GENE ENCODING; SIGNAL ENCODING; TRANSCRIPTION;

AMINO ACID SEQUENCE; DNA SEQUENCE ANALYSIS; GENES ENCODE; GENES ENCODING; GLUCOSIDASE; MOLECULAR CHARACTERIZATION; OPEN READING FRAME; SECONDARY STRUCTURES; STRUCTURAL CHARACTERIZATION; THERMOTOLERANT;

TOPOLOGY;

GLUCAN 1,4 ALPHA GLUCOSIDASE;

AMINO ACID SEQUENCE; ARTICLE; ENZYME ANALYSIS; MOLECULAR CLONING; NONHUMAN; OPEN READING FRAME; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; THERMOMONOSPORA;

ACTINOBACTERIA (CLASS); BACILLUS CEREUS; HORDEUM VULGARE SUBSP. VULGARE; THERMOMONOSPORA CURVATA; UNCULTURED ACTINOMYCETE;

EID: 0034024257     PISSN: 13645072     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2672.2000.01019.x     Document Type: Article

References (58)

1. Alber, T., Sun, D., Wilson, K., Wozniak, J.A., Cook, S.P. and Matthews, B.W. (1987) Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phageT4 lysozyme. Nature 330, 41-46.
2. Banner, D.W., Bloomer, A.C., Petsko, G.A. et al. (1975) Structure of chicken muscular triose phosphate isomerase determined crystallographically at 2.5 A° resolution. Nature 255, 609-614.
3. Blundell, T, Lindley, P., Miller, L. et al. (1981) The molecular structure and stability of the eye lens: X-ray analysis of γ-crystallin II. Nature 289, 771-777.
4. Boel, E., Brady, L., Brzozowski, A.M. et al. (1990) Calcium binding in α-amylases: an X-ray diffraction study at 2.1 A° resolution of two enzymes from Aspergillus. Biochemistry 29, 6244-6249.
5. Braver, G.D., Luo, Y. and Withers, S.G. (1995) The structure of human pancreatic α-amylase at 1.8 A° resolution and comparisons with related enzymes. Protein Science 4, 1730-1742.
6. Buisson, G., Duée, A., Haser, R. and Payan, F. (1987) Three dimensional structure of porcine pancreatic α-amylase at 2.9 A° resolution. Role of calcium in structure and activity. EMBO Journal 6, 3909-3916.
7. Busch, J.E., Porter, E.G. and Stutzenberger, F.J. (1997) Induction of α-amylase by maltooligosaccharides in Thermomonospora curvata. Journal of Applied Microbiology 82, 669-676.
8. Chiba, S., Saeki, T. and Shimomura, T. (1973) Substrate specificity of Saccharomyces logos α-glucosidase. Agricultural Biological Chemistry 37, 1831-1837.
9. Chou, P.Y. and Fasman, G.D. (1978) Empirical predications of protein conformation. Annual Review of Biochemistry 47, 251-276.
10. Collins, B.S., Kelly, C.T., Fogarty, W.M. and Doyle, E.M. (1993) The high maltose-producing α-amylase of the thermophilic actinomycete, Thermomonospora curvata. Applied Microbiology and Biotechnology 39, 31-35.
11. Duplay, P., Bedouelle, H., Fowler, I., Zabin, I., Saurin, W. and Hofnung, M. (1984) Sequences of the malE gene and of its product the maltose-binding protein of Escherichia coli K12. Journal of Biological Chemistry 259, 10606-10613.
12. Farber, K. and Petsko, G.A. (1990) The evolution of α/β barrel enzymes. TIBS 15, 228-234.
13. Garnier, J., Osguthorpe, D.J. and Robson, B. (1978) Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. Journal of Molecular Biology 120, 97-120.
14. Glymph, J.L. and Stutzenberger, F.J. (1977) Production, purification, and characterization of α-amylase from Thermomonospora curvata. Applied and Environmental Microbiology 34, 391-397.
15. Hopwood, D.A., Bibb, M.J., Chater, K.F. et al. (1985) Genetic Manipulation of Streptomyces. A Laboratory Manual. Norwich: John Innes Foundation.
16. Janda, L., Pavelka, T., Tichý, P., Spízek, J. and Petrícek, M. (1997) Production and properties of α-glucosidase from the thermophilic bacterium Thermomonospora curvata. Journal of Applied Microbiology 83, 470-476.
17. 8-barrel domains. Biochemical Journal 288, 1069-1070.
18. 8-barrel enzymes revealed by conserved regions of α-amylase. FEBS Letters 316, 23-26.
19. 8-barrel glycosyl hydrolases suggested by the similarity of their fifth conserved sequence region. FEBS Letters 377, 6-8.
20. Kadziola, A., Abe, J., Svensson, B. and Haser, R. (1994) Crystal and molecular structure of barley α-amylase. Journal of Molecular Biology 239, 104-121.
21. Kellis, J.T., Nyberg, K., Säli, D. and Fersht, A.R. (1988) Contribution of Hydrophobic interactions to protein stability. Nature 333, 784-786.
22. Kizaki, H., Hata, Y., Watanabe, K., Katsube, Y. and Suzuki, Y. (1993) Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 A° resolution X-ray analysis. Journal of Biochemistry 113, 646-649.
23. Kneller, D.G., Cohen, F.E. and Langridge, R. (1990) Improvements in protein secondary structure prediction by an enhanced neural network. Journal of Molecular Biology 214, 171-182.
24. Mac-Arthur, M.W. and Thornton, J.M. (1991) Influence of proline residues on protein conformation. Journal of Molecular Biology 218, 397-412.
25. MacGregor, E.A. and Svensson, B. (1989) A super-secondary structure predicted to be common to several α-1,4-D-glucan-cleaving enzymes. Biochemical Journal 259, 145-152.
26. Matsumura, M., Becktel, W.J., Levitt, M. and Matthews, B.W. (1989) Stabilization of phage T4 lysozyme by engineered disulfide bonds. Proceedings of the National Academy of Science USA 86, 6562-6566.
27. Matsuura, Y., Kusunoki, M., Harada, W. and Kakudo, M. (1984) Structure and possible catalytic residues of Taka-amylase A. Journal of Biochemistry 95, 697-702.
28. Matthews, B.W., Nicholson, W.H. and Becktel, W.J. (1987) Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proceedings of the National Academy of Science USA 84, 6663-6667.
29. McCarter, J.D. and Withers, S.G. (1996) Unequivocal identification of Asp-214 as the catalytic nucleophile of Saccharomyces cerevisiae α-glucosidase using 5-fluoro glycosyl fluorides. Journal of Biological Chemistry 271, 6889-6894.
30. Nakao, M., Nakayma, T., Kakudo, A. et al. (1994) Structure and expression of a gene coding for thermostable α-glucosidase with a broad substrate specificity from Bacillus sp. SAM1606. European Journal of Biochemistry 220, 293-300.
31. Petrícek, M., Stajner, K. and Tichý, P. (1989) Cloning of a thermostable α-amylase gene from Thermomonospora curvata and its expression in Streptomyces lividans. Journal of General Microbiology 135, 3303-3309.
32. Petrícek, M., Tichý, P. and Kuncová, M. (1992) Characterization of the α-amylase-encoding gene from Thermomonospora curvata. Gene 112, 77-83.
33. Puyet, A. and Espinosa, M. (1993) Structure of the maltodextrinuptake locus of Streptococcus pneumoniae. Journal of Molecular Biology 230, 800-811.
34. Qian, M., Haser, R. and Payan, F. (1993) Structure and molecular model refinement of pig pancreatic α-amylase at 2.1 A° resolution. Journal of Molecular Biology 231, 785-799.
35. Rimmele, M. and Boos, W. (1994) Trehalose-6-phosphate hydrolase of Escherichia coli. Journal of Bacteriology 176, 5654-5664.
36. Rost, B. and Sander, C. (1993) Prediction of protein secondary structure at better than 70% accuracy. Journal of Molecular Biology 232, 584-599.
37. Sambrook, J., Fritch, A.F. and Maniatis, T. (1989) Molecular Cloning: a laboratory Manual. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press.
38. Schwartz, M. (1987) The maltose regulon. In Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, Vol. 2 ed. Neidhardt, F.C., Ingham, J.L., Low, K.B., Magasnik, B., Shaechter, M. and Umbarger, H.E. pp. 1482-1502. Washington, D.C.: American Society for Microbiology.
39. Stutzenberger, F.J. (1972) Cellulolytic activity of Thermomonospora curvata: nutritional requirements for cellulase production. Applied Microbiology 24, 77-82.
40. Stutzenberger, F.J. (1987) Inducible thermoalkalophilic polygalacturonate lyase from Thermomonospora fusca. Journal of Bacteriology 169, 2774-2780.
41. Stutzenberger, F.J. and Bodine, A.B. (1992) Xylanase production by Thermomonospora curvata. Journal of Applied Bacteriology 72, 504-511.
42. Stutzenberger, F. and Carnell, R. (1977) Amylase production by Thermumimospora curvata. Applied and Environmental Microbiology 34, 234-236.
43. Stutzenberger, F.J., Kaufman, A.J. and Lossin, R.D. (1970) Cellulolytic activity in municipal solid waste composting. Canadian Journal of Microbiology 16, 553-560.
44. Suzuki, Y. (1989) A general principle of increasing protein thermostability. Proceedings of the Japan Academy Ser. B Physical and Biology Sciences 65, 146-148.
45. Suzuki, Y., Oishi, K., Nakano, H. and Nagayama,T. (1987) A strong correlation between the increase in number of proline residues and the rise in thermostability of five Bacillus oligo-1,6-glucosidases. Applied Microbiology and Biotechnology 26, 546-551.
46. Svensson, B. (1988) Regional distant sequence homology between amylases, α-glucosidases and transglucanosylases. FEBS Letters 230, 72-76.
47. Swift, H.J., Brady, L., Derewenda, Z.S. et al. (1991) Structure and molecular model refinement of Aspergillus oryzae (TAKA) α-amylase: an application of the simulated-annealing method. Acta Crystallographica 47, 535-544.
48. Takata, H., Kuriki,T., Okada, S. et al. (1992) Action of neopullulanase. Journal of Biological Chemistry 267, 18447-18452.
49. Tomazic, S.J. and Klibanov, A.M. (1988) Why is one Bacillus α-amylase more resistant against irreversible thermoinactivation than another? Journal of Biological Chemistry 263, 3092-3096.
50. van Wezel, G.P., White, J., Young, P., Postma, P.W. and Bibb, M.J. (1997a) Substrate induction and glucose repression of maltose utilisation by Streptomyces coelicolor A3 (2) is controlled by malR, a member of the lacI-galR. family of regulatory genes. Molecular Microbiology 23, 537-549.
51. van Wezel, G.P.,Whitte, J, Bibb, M.J. and Postma, P.W. (1997b) The malEFG gene cluster of Streptomyces coelicolor A3 (2): Characterization, disruption and transcriptional analysis. Molecular and General Genetic 254, 604-608.
52. Vihinen, M. and Mäntsälä, P. (1989) Microbial amylolytic enzymes. Critical Reviews in Biochemistry and Molecular Biology 24, 329-418.
53. Vogelstein, B. and Gillespie, D. (1979) Preparative and analytical purification of DNA from agarose. Proceedings of the National Academy of Sciences of the USA 76, 615-619.
54. Watanabe, K., Chishiro, K., Kitamura, K. and Suzuki, Y. (1991) Proline residue responsible for thermostability occurs with high frequency in the loop regions of an extremely thermostable oligo1,6-glucosidase from Bacillus thermoglucosidasius KP1006. Journal of Biological Chemistry 266, 24287-24294.
55. Watanabe, K., Hata, Y, Kizaki, H., Katsube, Y. and Suzuki, Y. (1997) The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 A° resolution: structural characterization of proline-substitution sites for protein thermostabilization. Journal of Molecular Biology 269, 142-153.
56. Watanabe, K., Kitamura, K., Iha, H. and Suzuki, Y. (1990) Primary structure of the oligo-1,6-glucosidase of Bacillus cereus ATCC 7064 deduced from the nucleotide sequence of the cloned gene. European Journal of Biochemistry 192, 609-620.
57. Watanabe, K., Kitamura, K. and Suzuki, Y. (1996). Analysis of the critical sites for protein thermostabilization by proline substitution in oligo-1,6-glucosidase from Bacillus coagulans ATCC 7050 and evolutionary consideration of proline residues. Applied and Environmental Microbiology 62, 2066-2073.
58. Watanabe, K., Masuda, T., Ohashi, H., Mihara, H. and Suzuki, Y. (1994) Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase. European Journal of Biochemistry 226, 277-283.