Preamylopectin processing: A mandatory step for starch biosynthesis in plants

Plant Cell

Volumn 8, Issue 8, 1996, Pages 1353-1366

  Mouille, Gregory ^a   Maddelein, Marie Lise ^a   Libessart, Nathalie ^b   Talaga, Philippe ^a   Decq, André ^a   Delrue, Brigitte ^a   Ball, Steven ^a  

^a UNIV LILLE   (France)

^b Roquette Freres   (France)

Author keywords

[No Author keywords available]

Indexed keywords

CHLAMYDOMONAS;

EID: 0029823269     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.8.8.1353     Document Type: Article

References (51)

1. Ball, S.G. (1995). Recent views on the biosynthesis of the starch granule. Trends Glycosci. Glycotechnol. 7, 405-415.
2. Ball, S.G., Dirick, L., Decq, A., Martiat, J.C., and Matagne, R.F. (1990). Physiology of starch storage in the monocellular alga Chlamydomonas reinhardtii. Plant Sci. 66, 1-9.
3. Ball, S., Marianne, T., Dirick, L., Fresnoy, M., Delrue, B., and Decq, A. (1991) A Chlamydomonas reinhardtii low-starch mutant is defective for 3-phosphoglycerate activation and orthophosphate inhibition of ADP-glucose pyrophosphorylase. Planta 185, 17-26.
4. Ball, S., Guan, H.-P., James, M., Myers, A., Keeling, P., Mouille, G., Buléon, A., Colonna, P., and Preiss, J. (1996) From glycogen to amylopectin: A model for the biogenesis of the plant starch granule. Cell, in press.
5. Banks, W., Greenwood, C.T., and Khan, K.M. (1971). The interaction of linear amylose oligomers with iodine. Carbohydr. Res. 17, 25-33.
6. Black, R.C., Loerch, J.D., McArdle, F.J., and Creech, R.G. (1966). Genetic interactions affecting maize phytoglycogen and the phytoglycogen-forming branching enzyme. Genetics 53, 661-668.
7. Boyer, C., and Preiss, J. (1978). Multiple forms of starch branching enzyme of maize: Evidence for independent genetic control. Biochem. Biophys. Res. Commun. 80, 169-175.
8. Caspar, T. (1994). Genetic dissection of the biosynthesis, degradation, and biological functions of starch. In Arabidopsis, Monograph 27, E.M. Meyerowitz and C. Somerville, eds (Cold Spring Harbor, NY Cold Spring Harbor Laboratory), pp. 913-936.
9. Caspar, T., Huber, S.C., and Somerville, C. (1985). Alterations in growth, photosynthesis, and respiration in a starchless mutant of Arabidopsis thaliana (L.) deficient in chloroplast phosphoglucomutase activity. Plant Physiol. 79, 11-17.
10. Delrue, B., Fontaine, T., Routier, F., Decq, A., Wieruszeski, J.M., Van den Koornhuyse, N., Maddelein, M.-L., Fournet, B., and Ball, S. (1992). Waxy Chlamydomonas reinhardtii: Monocellular algal mutants defective in amylose biosynthesis and granule-bound starch synthase accumulate a structurally modified amylopectin. J. Bacteriol. 174, 3612-3620.
11. Erlander, S. (1958). Proposed mechanism for the synthesis of starch from glycogen. Enzymologia 19, 273-283.
12. Fontaine, T., D'Hulst, C., Maddelein, M.-L., Routier, F., Marianne-Pepin, T., Decq, A., Wieruszeski, J.M., Delrue, B., Van den Koornhuyse, N., Bossu, J.P., Fournet, B., and Ball, S.G. (1993). Toward an understanding of the biogenesis of the starch granule: Evidence that Chlamydomonas soluble starch synthase II controls the synthesis of intermediate size glucans of amylopectin. J. Biol. Chem 268, 16223-16230
13. French, D. (1984). Organization of starch granules. In Starch, Chemistry and Technology, R L. Whistler, J.N. BeMiller, and E.F. Paschall, eds (New York: Academic Press), pp. 183-247.
14. Gabriel, O., and Gersten, D.M. (1992). Staining for enzymatic activity after gel electrophoresis, I. Anal. Biochem. 203, 1-21.
15. Geddes, R. (1985). Glycogen: A structural viewpoint In The Polysaccharides, Vol. 3, G O. Aspinall, ed (San Diego, CA: Academic Press), pp. 283-336
16. Gidley, M.J. (1985). Quantification of the structural features of starch polysaccharides by N.M.R spectroscopy. Carbohydr. Res 139, 85-93.
17. Guan, H.P., and Preiss, J. (1993). Differentiation of the properties of the branching isoenzymes from maize. Plant Physiol. 102, 1269-1273.
18. Guan, H.P., Kuriki, T., Sivak, M., and Preiss, J. (1995). Maize branching enzyme catalyzes synthesis of glycogen-like polysaccharide in glgB-deficient Escherichia coli. Proc. Natl. Acad. Sci. USA 92, 964-967.
19. Hanson, K.R., and McHale, N. A. (1988). A starchless mutant of Nicotiana sylvestris containing a modified plastid phosphoglucomutase. Plant Physiol. 88, 838-844.
20. Harris, E.H. (1989a). Genetic analysis. In The Chlamydomonas Sourcebook: A Comprehensive Guide to Biology and Laboratory Use, E Harris, ed (San Diego, CA: Academic Press), pp. 399-446.
21. Harris, E.H. (1989b). Culture and storage methods. In The Chlamydomonas Sourcebook: A Comprehensive Guide to Biology and Laboratory Use, E. Harris, ed (San Diego, CA Academic Press), pp. 25-63.
22. Harris, E.H. (1989c). Histological techniques for Chlamydomonas. In The Chlamydomonas Sourcebook: A Comprehensive Guide to Biology and Laboratory Use, E Harris, ed (San Diego, CA: Academic Press), pp. 581-586.
23. Iglesias, A.A., Charng, Y., Ball, S., and Preiss, J. (1994). Characterization of the kinetic, regulatory, and structural properties of ADP-glucose pyrophosphorylase from Chlamydomonas reinhardtii. Plant Physiol 104, 1287-1294.
24. Imberty, A., Buléon, A., Tran, V., and Pérez, S. (1991). Recent advances in knowledge of starch structure. Stärke 43, 375-384.
25. James, M.G., Robertson, D.S., and Meyers, A.M. (1995). Characterization of the maize gene sugaryl, a determinant of starch composition in kernels. Plant Cell 7, 417-429.
26. Jenkins, P.J., Cameron, R.E., and Donald, A.M. (1993). A universal feature in the starch granules from different botanical sources. Stärke 45, 417-420.
27. Kakefuda, G., and Duke, S.H. (1984). Electrophoretic transfer as a technique for the detection and identification of the plant amylolytic enzymes in polyacrylamide gels. Plant Physiol. 75, 278-280.
28. Kindle, K.L. (1990). High-frequency nuclear transformation of Chiamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA 87, 1228-1232.
29. Lacks, S.A., and Springhorn, S.S. (1980). Renaturation of enzymes after polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. J. Biol. Chem. 255, 7467-7473.
30. Lavintman, N. (1966). The formation of branched glucans in sweet corn. Arch. Biochem. Biophys. 116, 1-8.
31. Libessart, N., Maddelein, M.-L., Van den Koornhuyse, N., Decq, A., Delrue, B., Mouille, G., D'Hulst C., and Ball, S.G. (1995). Storage, photosynthesis and growth: The conditional nature of mutations affecting starch synthesis and structure in Chlamydomonas. Plant Cell 7, 1117-1127.
32. Lin, T.-P., Caspar, T., Somerville, C., and Preiss, J. (1988). Isolation and characterization of a starchless mutant of Arabidopsis thaliana (L.) Heynh. lacking ADP-glucose pyrophosphorylase activity. Plant Physiol 86, 1131-1135.
33. Maddelein, M.-L., Libessart, N., Bellanger, F., Delrue, B., D'Hulst, C., Van den Koornhuyse, N., Fontaine, T., Wieruszeski, J.M., Decq, A., and Ball, S.G, (1994) Toward an understanding of the biogenesis of the starch granule: Determination of granule-bound and soluble starch synthase functions in amylopectin synthesis. J. Biol. Chem. 269, 25150-25157.
34. Manners, D.J. (1968). Studies on carbohydrate metabolizing enzymes. Part XIX Sweet-corn branching enzymes. Carbohydr. Res. 8, 72-81
35. Manners, D.J. (1989) Recent developments in our understanding of amytopectin structure Carbohydr. Polymers 11, 87-112.
36. Müller-Röber, B., and Kossmann, J. (1994). Approaches to influence starch quantity and starch quality in transgenic plants. Plant Cell Environ. 17, 601-613.
37. Müller-Röber, B., Sonnewald, U., and Willmitzer, L. (1992). inhibition of the ADP-glucose pyrophosphorylase in transgenic potatoes leads to sugar-storing tubers and influences tuber formation and expression of tuber storage protein genes. EMBO J. 11, 1229-1238.
38. Nakamura, Y., Umemoto, T., Ogata, N., Kuboki, Y., Yano, M., and Saski, T. (1996a) Starch debranching enzyme (R-enzyme or pullulanase) from developing rice endosperm: Purification, cDNA and chromosomal localization of the gene. Planta 199, 203-218.
39. Nakamura, Y., Umemoto, T., Takahata, Y., Komae, K., Amano, E., and Satoh, H. (1996b). Changes in structure of starch and enzyme activities affected by sugary mutations in developing rice endosperm: Possible role of starch debranching enzyme in amylopectin biosynthesis Physiol Plant., in press.
40. Nelson, O.E., and Pan, D. (1995). Starch synthesis in maize endosperms Annu Rev. Plant Physiol. Plant Mol. Biol. 46, 475-496.
41. Pan, D., and Nelson, O.E. (1984). A debranching enzyme deficiency in endosperms of the Sugary-1 mutants of maize. Plant Physiol. 74, 324-328.
42. Preiss, J. (1991). Biology and molecular biology of starch synthesis and its regulation. In Oxford Surveys of Plant Molecular and Cell Biology, Vol 7, B.J. Miflin, ed (Oxford, UK Oxford University Press), pp. 59-114.
43. Preiss, J., and Sivak, M.N. (1996). Starch synthesis in sinks and sources. In Photoassimilate Distribution in Plants and Crops: Source-Sink Relationships, E. Zamski and A.A Schaffer, eds (New York: Marcel Dekker, Inc.), pp. 63-96.
44. 2-concentrating mechanism is correlated with the formation of the starch sheath around the pyrenoid of Chlamydomonas reinhardtii. Planta 195, 210-216.
45. Rammesmayer, G., and Praznik, W. (1992). Fast and sensitive staining method of Q-enzyme, α-amylase, R-enzyme, phosphorylase and soluble starch synthase separated by starch-polyacrylamide gel electrophoresis. J. Chromatogr. 623, 399-402.
46. Robin, J.P., Mercier, C., Charbonnière, R., and Guilbot, A. (1974) Lintnerized starches: Gel filtration and enzymatic studies of insoluble residues from prolonged acid treatment of potato starch. Cereal Chem. 51, 389-406.
47. Shannon, J.C., and Garwood, D.L. (1984). Genetics and physiology of starch development. In Starch: Chemistry and Technology, 2nd ed, R.L. Whistler, J.N Bemiller, and E.F Paschall, eds (Orlando, FL: Academic Press), pp. 25-86.
48. Sumner, J.B., and Somers, G.F. (1944) The water soluble polysaccharide of sweet corn. Arch. Biochem. 4, 4-7.
49. Takeda, Y., Guan, H.P., and Preiss, J. (1993). Branching of amylose by the branching isoenzymes of maize endosperm. Carbohydr. Res. 240, 253-263.
50. Tomalsky, D.S., and Krisman, C.R. (1987). The degree of branching in (α1,4)-(α1,6)-linked glucopolysaccharides is dependent on intrinsic properties of the branching enzymes. Eur. J. Biochem 168, 393-397.
51. Van den Koornhuyse, N., Libessart, N., Delrue, B., Zabawinski, C., Decq, A., Iglesias, A., Preiss, J., and Ball, S. (1996). Control of starch composition and structure through substrate supply in the monocellular alga Chlamydomonas reinhardtii J Biol. Chem 271, 16281-16287.