A novel type carbohydrate-binding module identified in α-glucan, water dikinases is specific for regulated plastidial starch metabolism

Biochemistry

Volumn 45, Issue 14, 2006, Pages 4674-4682

  Mikkelsen, René ^a   Suszkiewicz, Ken ^a   Blennow, Andreas ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; DEGRADATION; DNA; METABOLISM; STARCH; SUBSTRATES;

AMYLOPECTIN MOLECULE; GLUCAN SUBSTRATE; PHOSPHORYLATING ACTIVITY; WILD TYPE (WT);

ENZYME KINETICS;

ALPHA GLUCAN; AMYLASE; AMYLOPECTIN; AMYLOSE; ARGININE; CARBOHYDRATE; GLUCAN; PHOSPHOTRANSFERASE; RECOMBINANT DNA; STARCH; TRYPSIN; UNCLASSIFIED DRUG; WATER DIKINASE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOHYDRATE METABOLISM; CATALYSIS; DNA PURIFICATION; DNA SEQUENCE; ENZYME SPECIFICITY; NUCLEOTIDE SEQUENCE; PLASTID; POTATO; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PHOSPHORYLATION; TANDEM REPEAT;

PEPTIDE FRAGMENTS; PHOSPHOTRANSFERASES (PAIRED ACCEPTORS); PLASTIDS; PROTEIN BINDING; PROTEIN ENGINEERING; SOLANUM TUBEROSUM; STARCH;

SOLANUM TUBEROSUM;

EID: 33645670615     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051712a     Document Type: Article

References (37)

1. 31P-NMR, Starch/Staerke 46, 167-172.
2. Hizukuri, S., Tabata, S., and Nikuni, Z. (1970) Studies on starch phosphate Part 1. Estimation of glucose-6-phosphate residues in starch and the presence of other bound phosphate(s), Starch/Staerke 22, 338-343.
3. Blennow, A., Engelsen, S. B., Munck, L., and Møller, B. L. (1999) Starch molecular structure and phosphorylation investigated by a combined chromatographic and chemometric approach, Carbohydr. Polym. 41, 163-174.
4. Tabata, S., Nagata, K., and Hizukuri, S. (1975) Studies on starch phosphates. Part 3. On the esterified phosphates in some cereal starches, Starch/Staerke 27, 333-335.
5. Yu, T.-S., Kofler, H., Häusler, R. E., Hille, D., Flügge, H.-I., Zeeman, S. C., Smith, A. M., Kossmann, J., Lloyd, J., Ritte, G., Steup, M., Lue, W., Chen, J., and Weber, A. (2001) The Arabidopsis sex1 mutant is defective in the Rl protein, a general regulator of starch degradation in plants, and not in the chloroplast hexose transporter, Plant Cell 13, 1907-1918.
6. Ritte, G., Lloyd, J. R., Eckermann, N., Rottmann, A., Kossmann, J., and Steup, M. (2002) The starch-related R1 protein is an α-glucan, water dikinase, Proc. Natl. Acad. Sci. U.S.A. 99, 7166-7171.
7. Mikkelsen, R., Baunsgaard, L., and Blennow, A. (2004) Functional characterization of α-glucan, water dikinase, the starch phosphorylating enzyme, Biochem. J. 377, 525-532.
8. Mikkelsen, R., Mutenda, K. E., Mant, A., Schürmann, P., and Blennow, A. (2005) α-Glucan, water dikinase (GWD): A plastidic enzyme with redox-regulated and coordinated catalytic activity and binding affinity, Proc. Natl. Acad. Sci. U.S.A. 102, 1785-1790.
9. Ritte, G., Lorberth, R., and Steup, M. (2000) Reversible binding of the starch-related R1 protein to the surface of transitory starch, Plant J. 21, 387-391.
10. Mikkelsen, R., and Blennow, A. (2005) Functional domain organization of the potato α-glucan, water dikinase (GWD): Evidence for separate site catalysis as revealed by limited proteolysis and deletion mutants, Biochem. J. 385, 355-361.
11. Coutinho, P. M., and Henrissat, B. (1999) Carbohydrate-active enzymes: An integrated database approach, in Recent Advances in Carbohydrate Bioengineering (Gilbert, H. J., Davies, G. J., Henrissat, B., and Svensson, B., Eds.) pp 3-12, The Royal Society of Chemistry, Cambridge, U.K.
12. Svensson, B., Jespersen, H., Sierks, M. R., and MacGregor, E. A. (1989) Sequence homology between putative raw-starch binding domains from different starch-degrading enzymes, Biochem. J. 264, 309-311.
13. Janeček, Š., Svensson, B., and MacGregor, E. A. (2003) Relation between domain evolution, specificity, and taxonomy of the α-amylase family members containing a C-terminal starch-binding domain, Eur. J. Biochem. 270, 635-645.
14. Viksø-Nielsen, A., Blennow, A., Jørgensen, K., Kristensen, K. H., Jensen, A., and Møller, B. L. (2001) Structural, physicochemical, and pasting properties of starches from potato plants with repressed r1-gene, Biomacromolecules 2, 836-843.
15. Lorberth, R., Ritte, G., Willmitzer, L., and Kossmann, J. (1998) Inhibition of a starch-granule-bound protein leads to modified starch and repression of cold sweetening, Nat. Biotechnol. 16, 473-477.
16. Blennow, A., Engelsen, S. B., Nielsen, T. H., Baunsgaard, L., and Mikkelsen, R. (2002) Starch phosphorylation: A new front line in starch research, Trends Plant Sci. 7, 445-450.
17. Ritte, G., Scharf, A., Eckermann, N., Haebel, S., and Steup, M. (2004) Phosphorylation of transitory starch is increased during degradation, Plant Physiol. 135, 2068-2077.
18. Bradford, M. M. (1976) Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding, Anal. Biochem. 72, 248-254.
19. Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Goeke, N. M., Olson, B. J., and Klenk, D. C. (1985) Measurement of protein using bicinchoninic acid, Anal. Biochem. 150, 76-85.
20. Laemmli, U. K. (1970) Cleavage of structural proteins during assembly of head of bacteriophage-T4, Nature 227, 680-685.
21. Burnette, W. N. (1981) Western blotting: Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein-A, Anal. Biochem. 112, 195-203.
22. Blennow, A., Bay-Smidt, A. M., Wischmann, B., Olsen, C. E., and Møller, B. L. (1998) The degree of starch phosphorylation is related to the chain length distribution of the neutral and the phosphorylated chains of amylopectin, Carbohydr. Res. 307, 45-54.
23. Blennow, A., Viksø-Nielsen, A., and Morell, M. K. (1998) α-Glucan binding of potato-tuber starch-branching enzyme I as determined by tryptophan fluorescence quenching, affinity electrophoresis and steady-state kinetics, Eur. J. Biochem. 252, 331-338.
24. Fonda, M. L. (1976) Bromopyruvate inactivation of glutamate apodecarboxylase: Kinetics and specificity, J. Biol. Chem. 251, 229-235.
25. Fontana, A., Fassina, G., Vita, C., Dalzoppo, D., Zamai, M., and Zambonin, M. (1986) Correlation between sites of limited proteolysis and segmental mobility in thermolysin, Biochemistry 25, 1847-1851.
26. Yu, T. S., Zeeman, S. C., Thorneycroft, D., Fulton, D. C., Dunstan, H., Lue, W. L., Hegemann, B., Tung, S. Y., Umemoto, T., Chapple, A., Tsai, D. L., Wang, S. M., Smith, A. M., Chen, J., and Smith, S. M. (2005) α-Amylase is not required for breakdown of transitory starch in Arabidopsis leaves, J. Biol. Chem. 280, 9773-9779.
27. Simpson, P. J., Xie, H. F., Bolam, D. N., Gilbert, H. J., and Williamson, M. P. (2000) The structural basis for the ligand specificity of family 2 carbohydrate-binding modules, J. Biol. Chem. 275, 41137-41142.
28. Boraston, A. B., Bolam, D. N., Gilbert, H. J., and Davies, G. J. (2004) Carbohydrate-binding modules: Fine-tuning polysaccharide recognition, Biochem. J. 382, 769-781.
29. Williamson, M. P., Le Gal-Coëffet, M. F., Sorimachi, K., Furniss, C. S. M., Archer, D. B., and Williamson, G. (1997) Function of conserved tryptophans in the Aspergillus niger glucoamylase 1 starch binding domain, Biochemistry 36, 7535-7539.
30. Paldi, T., Levy, I., and Shoseyov, O. (2003) Glucoamylase starch-binding domain of Aspergillus niger B1: Molecular cloning and functional characterization, Biochem. J. 372, 905-910.
31. Penninga, D., vanderVeen, B. A., Knegtel, R. M. A., vanHijum, S. A. F. T., Rozeboom, H. J., Kalk, K. H., Dijkstra, B. W., and Dijkhuizen, L. (1996) The raw starch binding domain of cyclodextrin glycosyltransferase from Bacillus circulans strain 251, J. Biol. Chem. 271, 32777-32784.
32. Tester, R. F., Karkalas, J., and Qi, X. (2004) Starch: Composition, fine structure and architecture, J. Cereal Sci. 39, 151-165.
33. Blennow, A., Bay-Smidt, A. M., Olsen, C. E., and Møller, B. L. (1998) Analysis of starch-bound glucose 3-phosphate and glucose 6-phosphate using controlled acid treatment combined with high-performance anion-exchange chromatography, J. Chromatogr., A 829, 385-391.
34. Takeda, Y., and Hizukuri, S. (1981) Re-examination of the action of sweet-potato β-amylase on phosphorylated (1-4)-α-D-glucan, Carbohydr. Res. 89, 174-178.
35. Wiesenborn, D. P., Orr, P. H., Casper, H. H., and Tacke, B. K. (1994) Potato starch paste behaviour as related to some physical/chemical properties, J. Food Sci. 59, 644-648.
36. Ellis, R. P., Cochrane, M. P., Dale, M. F. D., Duffus, C. M., Lynn, S., Morrison, I. M., Prentice, R. D. M., Swanston, J. S., and Tiller, S. A. (1998) Starch production and industrial use, J. Sci. Food Agric. 77, 289-311.
37. Jobling, S. A., Westcott, R. J., Tayal, A., Jeffcoat, R., and Schwall, G. P. (2002) Production of a freeze-thaw-stable potato starch by antisense inhibition of three starch synthase genes, Nat. Biotechnol. 20, 295-299.