Characterization of chimeric enzymes constructed between two distinct α-Amylase cDNAs from cultured rice cells

Bioscience, Biotechnology and Biochemistry

Volumn 63, Issue 8, 1999, Pages 1329-1335

  Abe, Rei ^a   Yoshida, Kensuke ^a   Aoyagi, Masanobu ^a   Kasahara, Shin ^a   Nakajima, Tasuku ^a  

^a SOKA UNIVERSITY   (Japan)

Author keywords

Chimeric protein; Gene expression; Suspension cultured rice cells; amylase

Indexed keywords

AMYLASE; COMPLEMENTARY DNA; HYBRID PROTEIN; ISOENZYME; PLANT DNA;

AMINO ACID SEQUENCE; ARTICLE; CELL CULTURE; CYTOLOGY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; MOLECULAR CLONING; MOLECULAR GENETICS; RICE; SEQUENCE HOMOLOGY;

ALPHA-AMYLASE; AMINO ACID SEQUENCE; CELLS, CULTURED; CLONING, MOLECULAR; DNA, COMPLEMENTARY; DNA, PLANT; ESCHERICHIA COLI; ISOENZYMES; MOLECULAR SEQUENCE DATA; ORYZA SATIVA; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

BACTERIA (MICROORGANISMS); ORYZA SATIVA;

EID: 0033174657     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.1329     Document Type: Article

References (26)

1. Fernandez-Tarrago, J., Rodriguez-Bujan, M. C., and Nicolas, G., Starch degradation during germination of Civer arietinum L. seeds. Rev. Esp. FisioL, 34, 87-92 (1978).
2. Mitsui, T., Yamaguchi, J., and Akazawa, T., Physicochemical and serological characterization of rice Alpha-amylase isoforms and identification of their corresponding genes. Plant Physiol., 110, 1395-1404 (1996).
3. Chiba, Y., Ui, M., Kato, Y., Nakajima, T., and Ichishima, E., Two groups of intracellular Alpha-amylase isozymes from cultured rice cells. Phytochemistry, 29, 2075-2078 (1990).
4. Chiba, Y., Nieda, Y., Nakajima, T., and Ichishima, E., Unique enzymatic properties of Alpha-amylase-III from suspension-cultured rice cells. Agric. Biol. Chem., 55, 901-902 (1991).
5. Terashima, M., Katoh, S., Thomas, B. R., and Rodriguez, R. L., Characterization of rice Alpha-amylase isozymes expressed by Saccharomyces cerevisiae. Appl. Microbiol. Biotechnol., 43, 1050-1055 (1995).
6. Sogaard, M. and Svensson, B., Expression of cDNAs encoding barley Alpha-amylase 1 and 2 in yeast and characterization of the secreted proteins. Gene, 94, 173-179 (1990).
7. Terashima, M., Hosono, M., and Katoh, S., Functional roles of protein domains on rice Alpha-amylase activity. Appl. Microbiol. Biotechnol., 47, 364-367 (1997).
8. Vretblad, P., Immobilization of ligands for biospecific affinity chromatography via their hydroxyl groups. The cyclohexaamy-lose-betα-amylase system. FEBS Lett., 47, 86-89 (1974).
9. Chirgwin, J. M., Przybyla, A. E., MacDonald, R. J., and Rutter, W. J., Isolation of biologically active ribonucleic acid from sources enriched in ribonucléase. Biochemistry, 18, 5294-5299 (1979).
10. Frohman, M. A., Dush, M. K., and Martin, G. R., Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer. Proc. Natl. Acad. Sci. USA, 85, 8998-9002 (1988).
11. Nelson, N. J., A photometric adaptation of the Somogyi method for the determination of glucose. J. Biol. Chem., 153, 375-380 (1944).
12. Somogyi, M., Notes on sugar determination. J. Biol. Chem., 195, 19-23 (1952).
13. O’Neill, S. D., Kumagai, M. H., Majumdar, A., Huang, N., Sutliff, T. D., and Rodriguez, R. L., The Alpha-amylase genes in Oryza sativa: characterization of cDNA clones and mRNA expression during seed germination. Mol Gen. Genet., 221, 235-244 (1990).
14. Huang, N., Koizumi, N., Reinl, S., and Rodriguez, R. L., Structural organization and differential expression of rice Alpha-amylase genes. Nucleic. Acids. Res., 18, 7007-7014 (1990).
15. Okamoto, K. and Akazawa, T., Purification of Alpha-amylase and betα-amylase from endosperm tissues of germinating rice seeds. Agric. Biol. Chem., 42, 1364-1379 (1978).
16. Mitsui, T., Ueki, Y., and Igaue, I., Biosynthesis and secretion of Alpha-amylase by rice suspension-cultured cells: purification and characterization of Alpha-amylase isozyme H. Plant Physiol. Biochem., 31, 863-874 (1993).
17. Nakajima, R., Imanaka, T., and Aiba, S., Comparison of amino acid sequences of eleven different Alpha-amylases. Appl. Microbiol. Biotechnol., 23, 355-360 (1986).
18. Matsuura, Y., Kusunoki, M., Harada, W., Tanaka, N., Iga, Y., Yasuoka, N., Toda, H., Narita, K., and Kakudo, M., Molecular structure of taka-amylase A. I. Backbone chain folding at 3 A resolution. J. Biochem. (Tokyo), 87, 1555-1558 (1980).
19. Buisson, G., Duee, E., Haser, R., and Payan, F., Three dimensional structure of porcine pancreatic Alpha-amylase at 2.9 A resolution. Role of calcium in structure and activity. Embo J., 6, 3909-3016 (1987).
20. Juge, N., Andersen, J. S., Tull, D., Roepstorff, P., and Svensson, B., Overexpression, purification, and characterization of recombinant barley Alpha-amylases 1 and 2 secreted by the methylotrophic yeast Pichia pastoris. Protein Expr. Purif., 8, 204-214 (1996).
21. Kumagai, M. H., Shah, M., Terashima, M., Vrkljan, Z., Whitaker, J. R., and Rodriguez, R. L., Expression and secretion of rice Alpha-amylase by Saccharomyces cerevisiae. Gene, 94, 209-216 (1990).
22. Sogaard, M., Construction of yeast expression systems allowing protein engineering of barley Alpha-amylase 1 and 2. M. Sc, Thesis, University of Copenhagen, (1989).
23. Schein, C. H. and Noteborn, M. H. M., Formation of soluble recombinant proteins in Escherichia coli, is favored by lower growth temperature. Biol technology, 6, 291-294 (1988).
24. Totsuka, A. and Fukazawa, C., Expression and mutation of soybean betα-amylase in Escherichia coli. Eur. J. Biochem., 214, 787-794 (1993).
25. Chou, P. Y. and Fasman, G. D., Prediction of the secondary structure of proteins from their amino acid sequence. Adv. En-zymol. Relat. Areas Mol. Biol., 47, 145-148 (1978).
26. Kadziola, A., Abe, J., Svensson, B., and Haser, R., Crystal and molecular structure of barley Alpha-amylase. J. Mol. Biol., 239, 104-121 (1994).