Characterization of a rice β-glucosidase highly expressed in flower and germinating shoot

Plant Science

Volumn 165, Issue 3, 2003, Pages 627-638

  Opassiri, Rodjana ^a   Ketudat Cairns, James R ^a   Akiyama, Takashi ^b   Wara Aswapati, Onnop ^a   Svasti, Jisnuson ^c   Esen, Asim ^d  

^a SURANAREE UNIVERSITY OF TECHNOLOGY   (Thailand)

^b NATIONAL AGRICULTURAL RESEARCH CENTER FOR HOKKAIDO REGION   (Japan)

^c MAHIDOL UNIVERSITY   (Thailand)

^d VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

Author keywords

Expression; Gluco oligosaccharides; Glycosides; Rice; Substrate specificity; Glucosidase

Indexed keywords

CLONING; DNA; ENZYMES; HYDROLYSIS;

GERMINATING SHOOTS;

PLANTS (BOTANY);

ESCHERICHIA COLI; ORYZA SATIVA;

EID: 0042130165     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9452(03)00235-8     Document Type: Article

References (45)

1. B. Henrissat, A classification of glycosyl hydrolases based on amino acid sequence similarities, Biochem. J. 280 (1991) 309-316.
2. B. Henrissat, A. Bairoch, New families in the classification of glycosyl hydrolases based on amino acid sequence similarities, Biochem. J. 293 (1993) 781-788.
3. B. Henrissat, A. Bairoch, Updating the sequence-based classification of glycosyl hydrolases, Biochem. J. 316 (1996) 695-696.
4. T. Barrett, C.G. Suresh, S.P. Tolley, E.J. Dodson, M.A. Hughes, The crystal structure of a cyanogenic β-glucosidase from white clover, a family 1 glycosyl hydrolase, Structure 3 (1995) 951-960.
5. B. Henrissat, I. Callebaut, S. Fabrega, P. Lehn, J.-P. Mornon, G. Davies, Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases, Proc. Natl. Acad. Sci. USA 92 (1995) 7090-7094.
6. J. Jenkins, L.L. Leggio, G. Harris, R. Pickersgill, Glucosidase, β-galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes with 8-fold β/α architecture and with two conserved glutamates near the carboxy-terminal ends of β-strands four and seven, FEBS Lett. 362 (1995) 281-285.
7. M. Czjzek, M. Cicek, V. Zamboni, W.P. Burmeister, D.R. Bevan, B. Henrissat, A. Esen, The mechanism of substrate (aglycone) specificity in β-glucosidases is revealed by crystal structures of mutant maize β-glucosidase-DIMBOA, -DIMBOAGIc, and -dhurrin complexes, Proc. Natl. Acad. Sci. USA 97 (2000) 13555-13560.
8. M. Czjzek, M. Cicek, V. Zamboni, W.P. Burmeister, D.R. Bevan, B. Henrissat, A. Esen, Crystal structure of a monocotyledon (maize ZMGIu1) β-glucosidase and a model of its complex with p-nitrophenyl β-D-thioglucoside, Biochem. J. 354 (2001) 37-46.
9. J.R. Ketudat Cairns, V. Champattanachai, C. Srisomsap, B. Thiede, B. Wittman-Liebold, J. Svasti, Sequence and expression of Thai rosewood β-glucosidase/β-fucosidase, a family 1 glycosyl hydrolase glycoprotein, J. Biochem. 128 (2000) 999-1008.
10. Z. Keresztessy, K. Brown, M.A. Dunn, M.A. Hughes, Identification of essential active-site residues in the cyanogenic β-glucosidase (linamarase) from cassava (Manihot esculenta Crantz) by site-directed mutagenesis, Biochem. J. 353 (2001) 199-205.
11. J.E. Poulton, Cyanogenesis in plants, Plant Physiol. 94 (1990) 401-405.
12. A. Nisius, The stromacentre in Avena plastids: an aggregation of β-glucosidase responsible for the activation of oat-leaf saponins, Planta 173 (1988) 474-481.
13. L. Duroux, F.M. Delmotte, J.-M. Lancelin, G. Keravis, C. Jay-Alleand, Insight into naphthoquinone metabolism: β-glucosidase-catalysed hydrolysis of hydrojuglone β-D-glucopyranoside, Biochem. J. 333 (1998) 275-283.
14. G.D. Babcock, A. Esen, Substrate specificity of maize β-glucosidase, Plant Sci. 101 (1994) 31-39.
15. J. Svasti, C. Srisomsap, S. Techasakul, R. Surarit, Dalcochinin-8′-O-β-D-glucoside and its β-glucosidase enzyme from Dalbergia cochinchinensis, Phytochemistry 50 (1999) 739-743.
16. 4-17-O-β-D-glucopyranoside, from rice anthers, Phytochemistry 37 (1994) 629-634.
17. T. Yokota, N. Murofushi, N. Takahashi, Structure of new gibberellin glucoside in immature seeds of Pharbitis nil, Tetrahedron Lett. 18 (1970) 1489-1491.
18. W.P. Burrow, D.P. Leworthy, Metabolism of N,N′-diphenylurea by cytokinin- dependent tobacco callus: identification of the glucoside, Biochem. Biophys. Res. Commun. 70 (1976) 1109-1114.
19. B. Brzobohaty, I. Moore, P. Kristoffersen, L. Bako, N. Campos, J. Schell, K. Palme, Release of active cytokinin by a β-glucosidase localized to the maize root meristem, Science 262 (1993) 1051-1054.
20. A. Falk, L. Rask, Expression of a zeatin-O-glucoside-degrading β-glucosidase in Brassica napus, Plant Physiol. 108 (1995) 1369-1377.
21. W. Schliemann, Hydrolysis of conjugated gibberellins by β-glucosidases from dwarf rice (Oryza sativa L. cv. Tan-ginbozu), J. Plant Physiol. 116 (1984) 123-132.
22. R. Leah, J. Kigel, I. Svedsen, J. Mundy, Biochemical and molecular characterization of a barley seed β-glucosidase, J. Biol. Chem. 270 (1995) 15789-15797.
23. T. Akiyama, H. Kaku, N. Shibuya, A cell wall-bound β-glucosidase from germinated rice: purification and properties, Phytochemistry 48 (1998) 49-54.
24. A. Geerlings, M. Matinez-Lozano Ibañez, J. Memlink, R. van der Heijden, R. Verpoorte, Molecular cloning and analysis of strictosidine β-D-glucosidase, an enzyme in terpeoid indole alkaloid biosynthesis in Catharanthus roseoux, J. Biol. Chem. 275 (2000) 3051-3056.
25. J.F. Gregory, Nutrition properties and significance of vitamin glycosides, Annu. Rev. Nutr. 18 (1998) 277-296.
26. E.P. Palmiano, B.O. Juliano, Changes in the activity of some hydrolases, peroxidase and catalase in rice seed during germination, Plant Physiol. 52 (1973) 274-277.
27. S.F. Altschul, T.L. Madden, A.A. Schäffer, J. Zhang, Z. Zhang, W. Miller, D.J. Lipman, Gapped BLAST and PSI-BLAST: a new generation of protein database search programs, Nucleic Acids Res. 25 (1997) 3389-3402.
28. Y. Zhang, M.A. Frohman, Using rapid amplification of cDNA ends (RACE) to obtain full-length cDNAs, in: I.G. Cowell, C.A. Austin (Eds.), cDNA Library Protocols, Humana Press, Totowa, New Jersey, 1997, pp. 61-87.
29. F. Jeanmougin, J.D. Thompson, M. Gouy, D.G. Higgins, T.J. Gibson, Multiple sequence alignment with Clustal X, Trends Biochem. Sci. 23 (1998) 403-405.
30. J.D. Thompson, D.G. Higgins, T.J. Gibson, CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions- specific gap penalties and weight matrix choice, Nucleic Acids Res. 22 (1994) 4673-4680.
31. H. Nielsen, J. Engelbrecht, S. Brunak, G. von Heijne, Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites, Protein Eng. 10 (1997) 1-6.
32. K. Nakai, P. Horton, PSORT: a program for detecting the sorting signals of proteins and predicting their subcellular localization, Trends Biochem. Sci. 24 (1999) 34-35.
33. J.J. Doyle, J.L. Doyle, A rapid DNA isolation procedure for small quantities of fresh leaf tissue, Phytochem. Bull. 19 (1987) 11-15.
34. J. Sambrook, E.F. Fritsch, T. Maniatis, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, New York, 1989, pp. 9.31-9.62.
35. C.W. Bachem, R.S. van der Hoeven, S.M. de Bruijn, D. Vreugdenhil, M. Zabeau, R.G. Visser, Visualization of differential gene expression using a novel method of RNA fingerprinting based on AFLP: analysis of gene expression during potato tuber development, Plant J. 9 (1996) 745-753.
36. J. Sambrook, E.F. Fritsch, T. Maniatis, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, New York, 1989, pp. 7.37-7.52.
37. G. Simos, C.A. Panagiotidis, A. Skoumbas, D. Choli, C. Ouzounis, J.G. Georgatsos, Barley β-glucosidase: expression during seed germination and maturation and partial amino acid sequences, Biochim. Biophys. Acta 1199 (1994) 52-58.
38. K. Yasumoto, H. Tsuji, K. Iwami, H. Mitsuda, Isolation from rice bran of a bound form of vitamin B6 and its identification as 5′-O-β-D-glucopyranosyl-pyridoxine, Agric. Biol. Chem. 41 (1977) 1061-1067.
39. J.F. Gregory, Nutrition properties of pyridoxine-β-glucosides, in: A. Esen (Ed.), β-Glucosidase, American chemical Society, Washington, DC, 1993, pp. 113-131.
40. M. Hrmova, A.J. Harvey, J. Wang, N.J. Shirley, G.P. Jones, B.A. Stone, P.B. Hoj, G.B. Fincher, Barley β-D-glucan exohydrolases with β-D-glucosidase activity, J. Biol. Chem. 271 (1996) 5277-5286.
41. M. Hrmova, E.A. MacGregor, P. Biely, R.J. Stewart, G.B. Fincher, Substrate binding and catalytic mechanism of a barley β-D-glucosidase/(1,4)-β-D-glucan exohydrolase, J. Biol. Chem. 273 (1998) 11134-11143.
42. M. Hrmova, G.B. Fincher, Plant enzyme structure. Explaining substrate specificity and the evolution of function, Plant Physiol. 125 (2001) 54-57.
43. S.A. Goff, D. Ricke, T.-H. Lan, G. Presting, R. Wang, M. Dunn, J. Glazebrook, A. Sessions, P. Oeller, H. Varma, et al., A draft sequence of the rice genome (Oryza sativa L. ssp. japonica), Science 296 (2002) 92-100.
44. J. Yu, S. Hu, J. Wang, G.K.-S. Wong, S. Li, B. Liu, Y. Deng, L. Dai, Y. Zhou, X. Zhang, et al., A draft sequence of the rice genome (Oryza sativa L. ssp. indica), Science 296 (2002) 79-92.
45. K.B. Nicholas, H.B. Nicholas, Jr., D.W. Decrfield, II, GeneDoc: analysis and visualization of genetic variation, EMBNEW.NEWS 4 (1997) 14.