Lysine-81 and threonine-82 on maize β-glucosidase isozyme Glu1 are the key amino acids involved in β-Glucosidase aggregating factor binding

Biochemistry

Volumn 48, Issue 13, 2009, Pages 2924-2932

  Yu, Hyun Young ^a   Kittur, Farooqahmed S ^a   Bevan, David R ^a   Esen, Asim ^a  

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

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ABILITIES; FOUR AMINO ACIDS; FRONTAL AFFINITY CHROMATOGRAPHIES; GLUCOSIDASE; HIGH MOLECULAR WEIGHTS;

AFFINITY CHROMATOGRAPHY; AMINATION; AMINO ACIDS; CHROMATOGRAPHIC ANALYSIS; GELATION; GELS; ORGANIC ACIDS;

AMINES;

AMINO ACID; BETA GLUCOSIDASE; BETA GLUCOSIDASE AGGREGATING FACTOR; GLUCOSIDASE; GLUTAMINE; ISOENZYME; LYSINE; THREONINE; UNCLASSIFIED DRUG;

AFFINITY CHROMATOGRAPHY; ARTICLE; COMPLEX FORMATION; MAIZE; MOLECULAR WEIGHT; MUTANT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN INTERACTION; SORGHUM; SUBSTITUTION REACTION;

AMINO ACID SEQUENCE; BETA-GLUCOSIDASE; CARRIER PROTEINS; CHROMATOGRAPHY, AFFINITY; CLONING, MOLECULAR; ELECTROPHORETIC MOBILITY SHIFT ASSAY; ISOENZYMES; LYSINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; PLANT PROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, PROTEIN; STRUCTURE-ACTIVITY RELATIONSHIP; THREONINE; ZEA MAYS;

ZEA MAYS;

EID: 65249096067     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900012h     Document Type: Article

References (34)

1. Reese, E. T. (1977) Degradation of polymeric carbohydrates by microbial enzymes. Recent Adv. Phytochem. 11, 311-368.
2. Poulton, J. E. (1990) Cyanogenesis in plants 1. Plant Physiol. 94, 401-405.
3. Phillips, D. A., and Streit, W. R. (1996) Legume signals to rhizobial symbionts: A new approach for defining rhizosphere colonization. Plant-Microbe Interact., 236-271.
4. Hughes, M. A., Brown, K., Pancoro, A., Murray, B. S., Oxtoby, E., and Hughes, J. (1992) A molecular and biochemical analysis of the structure of the cyanogenic β-glucosidase (linamarase) from cassava (Manihot esculenta Cranz). Arch. Biochem. Biophys. 295, 273-279.
5. Kahler, A. L., and Wehrhahn, C. F. (1986) Associations between quantitative traits and enzyme loci in the F2 population of a maize hybrid. Theor. Appl. Genet. 72, 15-26.
6. Massardo, F., Zuniga, G. E., Perez, L. M., and Corcuera, L. J. (1994) Effects of hydroxamic acids on electron transport and their cellular location in corn. Phytochemistry 35, 873-876.
7. Hosel, W., Surholt, E., and Borgmann, E. (1978) Characterization of β-glucosidase isoenzymes possibly involved in lignification from chick pea (Cicer arietinum L.) cell suspension cultures. FEBS J. 84, 487-492.
8. Dharmawardhana, D. P., Ellis, B. E., and Carlson, J. E. (1995) A β-glucosidase from lodgepole pine xylem specific for the lignin precursor coniferin. Plant Physiol. 107, 331-339.
9. Escamilla-Trevi, L. L., Chen, W., Card, M. L., Shih, M. C., Cheng, C. L., and Poulton, J. E. (2006) Arabidopsis thaliana β-glucosidases BGLU45 and BGLU46 hydrolyse monolignol glucosides. Phy-tochemistry 67, 1651-1660.
10. Koes, R. E., Quattrocchio, F., and Mol, J. N. M. (1994) The flavonoid biosynthetic pathway in plants: function and evolution. BioEssays 16, 123-132.
11. Kleczkowski, K., and Schell, J. (1995) Phytohormone conjugates: Nature and function. Crit. Rev. Plant Sci. 14, 283-298.
12. Lee, K. H., Piao, H. L., Kim, H. Y., Choi, S. M., Jiang, F., Hartung, W., Hwang, I., Kwak, J. M., Lee, I. J., and Hwang, I. (2006) Activation of glucosidase via stress-induced polymerization rapidly increases active pools of abscisic acid. Cell 126, 1109-1120.
13. Kristoffersen, P., Brzobohaty, B., Hohfeld, I., Bako, L., Melkonian, M., and Palme, K. (2000) Developmental regulation of the maize Zm-p60.1 gene encoding a β-glucosidase located to plastids. Planta 210, 407-415.
14. Mizutani, M., Nakanishi, H., Ema, J., Ma, S., Noguchi, E., Inohara-Ochiai, M., Fukuchi-Mizutani, M., Nakao, M., and Sakata, K. (2002) Cloning of β-primeverosidase from tea leaves, a key enzyme in tea aroma formation. Plant Physiol. 130, 2164-2176.
15. Fia, G., Giovani, G., and Rosi, I. (2005) Study of β-glucosidase production by wine-related yeasts during alcoholic fermentation. A new rapid fluorimetric method to determine enzymatic activity. J. Appl. Microbiol. 99, 509-517.
16. Van Remsburg, P., Van Zyl, W., and Pretorius, I. (1998) Engineering yeast for efficient cellulose degradation. Yeast 14, 67-76.
17. Esen, A., and Blanchard, D. J. (2000) A specific β-glucosidase- aggregating factor is responsible for the β-glucosidase null phenotype in maize. Plant Physiol. 122, 563-572.
18. Kittur, F. S., Lalgondar, M., Yu, H. Y., Bevan, D. R., and Esen, A. (2007) Maize β-glucosidase-aggregating factor is a polyspecific jacalin-related chimeric lectin, and its lectin domain is responsible for β-glucosidase aggregation. J. Biol. Chem. 282, 7299-7311.
19. Subramanyam, S., Smith, D. F., Clemens, J. C., Webb, M. A., Sardesai, N., and Williams, C. E. (2008) Functional characterization of HFR1, a high-mannose N-glycan-specific wheat lectin induced by Hessian fly larvae. Plant Physiol. 147, 1412-1426.
20. Cicek, M., and Esen, A. (1998) Structure and expression of a dhurrinase (β-glucosidase) from sorghum. Plant Physiol. 116, 1469-1478.
21. Blanchard, D. J., Cicek, M., Chen, J., and Esen, A. (2001) Identification of β-glucosidase aggregating factor (BGAF) and mapping of BGAF binding regions on maize β-glucosidase. J. Biol. Chem. 276, 11895-11901.
22. Cicek, M., Blanchard, D., Bevan, D. R., and Esen, A. (2000) The aglycone specificity-determining sites are different in 2,4-dihy-droxy-7-methoxy-1, 4-benzoxazin-3-one (DIMBOA)-glucosidase (maize β-glucosidase) and dhurrinase (sorghum β-glucosidase). J. Biol. Chem. 275, 20002-20011.
23. Cicek, M., and Esen, A. (1999) Expression of soluble and catalytically active plant (monocot) β-glucosidases in E. coli. Biotechnol. Bioeng. 63, 392-400.
24. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
25. Ohyama, Y., Kasai, K., Nomoto, H., and Inoue, Y. (1985) Frontal affinity chromatography of ovalbumin glycoasparagines on a concanavalin A-Sepharose column. A quantitative study of the binding specificity of the lectin. J. Biol. Chem. 260, 6882-6887.
26. Coneva, V., Zhu, T., and Colasanti, J. (2007) Expression differences between normal and indeterminatel maize suggest downstream targets of ID1, a floral transition regulator in maize. J. Exp. Bot. 58, 3679-3693.
27. Eriksson, S., Andreasson, E., Ekbom, B., Graner, G., Pontoppidan, B., Taipalensuu, J., Zhang, J., Rask, L., and Meijer, J. (2002) Complex formation of myrosinase isoenzymes in oilseed rape seeds are dependent on the presence of myrosinase-binding proteins. Plant Physiol. 129, 1592-1599.
28. Nagano, A. J., Matsushima, R., and Hara-Nishimura, I. (2005) Activation of an ER-body-localized β-glucosidase via a cytosolic binding partner in damaged tissues of Arabidopsis thaliana. Plant Cell Physiol. 46, 1140-1148.
29. Taipalensuu, J., Eriksson, S., and Rask, L. (1997) The myrosinase-binding protein from Brassica napus seeds possesses lectin activity and has a highly similar vegetatively expressed wound-inducible counterpart. Eur. J. Biochem. 250, 680-688.
30. Chen, S., and Halkier, B. A. (1999) Functional expression and characterization of the myrosinase MYR1 from Brassica napus in Saccharomyces cerevisiae. Protein Expression Purif. 17, 414-420.
31. Andreasson, E., Jorgensen, L. B., Hoglund, A. S., Rask, L., and Meijer, J. (2001) Different myrosinase and idioblast distribution in Arabidopsis and Brassica napus. Plant Physiol. 127, 1750-1763.
32. Williams, C. E., Collier, C. C., Nemacheck, J. A., Liang, C., and Cambron, S. E. (2002) A lectin-like wheat gene responds systemi-cally to attempted feeding by avirulent first-instar hessian fly larvae. J. Chem. Ecol. 28, 1411-1428.
33. Gorlach, J., Volrath, S., Knauf-Beiter, F., Hengry, G., Beckhove, U., Kogel, K. H., Oostendorp, M., Staub, T., Ward, E., and Kessmann, H. (1996) Benzonthiazole, a novel class of inducers of systemic acquired resistance, actives gene expression and disease resistance on wheat. Plant Cell 8, 629-643.
34. Chisholm, S. T., Parra, M. A., Anderberg, R. J., and Carrington, J. C. (2001) Arabidopsis RTM1 and RTM2 genes function in phloem to restrict long-distance movement of tobacco etch virus. Plant Physiol. 127, 1667-1675.