N- and C-terminal peptide sequences are essential for enzyme assembly, Allosteric, and/or catalytic properties of ADP-glucose pyrophosphorylase

Plant Journal

Volumn 14, Issue 2, 1998, Pages 159-168

  Laughlin, Mary J ^a,b   Chantler, Sue Ellen ^a   Okita, Thomas W ^a  

^a Institute of Biological Chemistry   (United States)

^b WASHINGTON STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERISM; ENZYME ACTIVITY; ENZYME REGULATION; GLUCOSE 1 PHOSPHATE ADENYLYLTRANSFERASE;

ALLOSTERIC REGULATION; AMINO ACID SEQUENCE; AMINO ACIDS; CATALYSIS; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE; HEAT; KINETICS; MOLECULAR SEQUENCE DATA; NUCLEOTIDYLTRANSFERASES; PEPTIDE FRAGMENTS; SEQUENCE DELETION; SOLANUM TUBEROSUM; SPINACIA OLERACEA;

ESCHERICHIA; SOLANUM TUBEROSUM;

EID: 0032052136     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.1998.00102.x     Document Type: Article

References (31)

1. Ball, K. and Preiss, J. (1994) Allosteric sites of the large subunit of the spinach leaf ADPglucose pyrophosphorylase. J. Biol. Chem. 269, 24706-24711.
2. Ballicora, M.A., Laughlin, M.J., Fu, Y., Okita, T.W., Barry, G.F. and Preiss, J. (1995) Adensine 5′-diphosphate-glucose pyrophosphorylase from potato tuber: significance of the N-terminus of the small subunit for catalytic properties and heat stability. Plant Physiol. 109, 245-251.
3. 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.
4. Denyer, K., Dunlap, F., Thorbjørnsen, T., Keeling, P. and Smith, A.M. (1996) The Major form of ADP-glucose pyrophosphorylase in maize endosperm is extra-plastidial. Plant Physiol. 112, 779-785.
5. Dickinson, D. and Preiss, J. (1981) ADPglucose pyrophosphorylases from maize endosperm. Arch. Biochem. Biophys. 130, 119-128.
6. Giroux, M.J., Shaw, J., Barry, G., Cobb, B.G., Greene, T., Okita, T. and Hannah, L.C. (1996) A single gene mutation that increases maize seed weight. Proc. Natl Acad. Sci. USA, 93, 5824-5829.
7. Greene, T.W., Chantier, S.E., Kahn, M.L., Barry, G.F., Preiss, J. and Okita, T.W. (1996a) Mutagenesis of the potato tuber ADPglucose pyrophosphorylase and characterization of an allosteric mutant defective in 3-phosphoglycerate activation. Proc. Natl Acad. Sci. USA, 33, 1509-1513.
8. Greene, T.W., Woodbury, R.L. and Okita, T.W. (1996b) Aspartic acid 413 is important for the normal allosteric functioning of ADP-glucose pyrophosphorylase. Plant Physiol. 112, 1315-1320.
9. Hylton, C. and Smith, A.M. (1992) The rb mutation of peas causes strcutural and regulatory changes in ADP glucose pyrophosphorylase deom developing embryos. Plant Physiol. 99, 1626-1634.
10. Iglesias, A.A., Barry, G.F., Meyer, C., Bloksberg, L., Nakata, P.A., Greene, T., Laughlin, M.J., Okita, T.W., Kishore, G.M. and Preiss, J. (1993) Expression of the potato tuber ADP-glucose pyrophosphorylase in Escherichia coli. J. Biol. Chem. 268, 1081-1086.
11. Kleczkowski, L.A., Villand, P., Luthi, E., Olsen, O.-A. and Preiss, J. (1993) Insensitivity of barley endosperm ADP-glucose pyrophosphorylase to 3-phosphoglycerate and orthophosphate regulation. Plant Physiol. 101, 179-186.
12. Laughlin, M.J., Payne, J.W. and Okita, T.W. (1998) The generation of substrate binding mutants of the higher plant ADP-glucose pyrophosphorylase by random mutagenesis. Phytochemistry, 47, 621-629.
13. Martin, C. and Smith, A.M. (1995) Starch synthesis. Plant Cell, 7, 971-985.
14. Morell, M., Bloom, M. and Preiss, J. (1988) Affinity labeling of the allosteric activator site (s) of spinach leaf ADP-glucose pyrophosphorylase. J. Biol. Chem. 263, 633-637.
15. Nakata, P.A., Greene, T.W., Anderson, J.M., Smith-White, B.J., Okita, T.W. and Preiss, J. (1991) Comparison of the primary sequences of the two potato tuber ADP-glucose pyrophosphorylase subunits. Plant Mol. Biol. 17, 1089-1093.
16. Neuhaus, H.E. and Stitt, M. (1990) Control. analysis of photosynthate partitioning: Impact of reduced activity of ADP-glucose pyrophosphorylase or plastid phosphoglucomutase on the fluxes to starch and sucrose in Arabidopsis thaliana (L.) Heynh. Planta, 182, 445-454.
17. Okita, T.W. (1992) Is there an alternative pathway for starch synthesis? Plant Physiol. 100, 560-564.
18. Okita, T.W., Nakata, P.A., Anderson, J.M., Sowokinos, J., Morell, M. and Preiss, J. (1990) The subunit structure of potato tuber ADPglucose pyrophosphorylase. Plant Physiol. 93, 785-790.
19. Okita, T.W., Nakata, P., Smith-White, B. and Preiss, J. (1993) Enhancement of plant productivity by manipulation of ADPglucose pyrophosphorylase. In Gene Conservation and Exploitation (J. P. Gustafson, ed.). New York: Plenum Press, pp. 161-191.
20. Olive, M., Ellis, R.J. and Schuch, W.W. (1989) Isolation and nucletoide sequences of cDNA clones encoding ADP-glucose pyrophosphorylase polypeptides from wheat leaf and endosperm. Plant Mol. Biol. 12, 525-538.
21. Plaxton, W.C. and Preiss, J. (1987) Purification and properties of nonproteolytic degraded ADPglucose pyrophosphorylase from maize endosperm. Plant Physiol. 83, 105-112.
22. Preiss, J. (1992) Biology and molecular biology of starch synthesis and its regulation. In Oxford Surveys of Plant Molecular and Cellular Biology, Vol. 7 (B. J. Miflin, ed.). Oxford: Oxford University Press, pp. 59-114.
23. Preiss, J., Ballicora, M.A., Laughlin, M.J., Fu, Y., Okita, T.W., Barry, G.F., Guan, H. and Sivak, M.N. (1995) Studies on the starch biosynthetic enzymes for manipulation of starch content and quality. In Carbon Partitioning and Source-Sink Interactions in Plants (W. J. Lucas, ed.). Rockville: American Society of Plant Physiologists, pp. 91-101.
24. Preiss, J., Hutney, J., Smith-White, B., Li, L. and Okita, T.W. (1991) Regulatory mechanisms involved in the biosynthesis of starch. J. Pure Appl. Chem. 63, 535-544.
25. Preiss, J. and Romeo, T. (1994) Molecular biology and regulatory aspects of glycogen biosynthesis in bacteria. In Progress in Nucleic Acid Research and Molecular Biology, Vol 47 (W.E. Cohn K. Moldave, eds.). San Diego: Academic Press Inc., pp. 299-329.
26. Preiss, J. and Sivak, M. (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: Dekker, pp. 139-168.
27. Smith-White, B.J. and Preiss, J. (1992) Comparison of Proteins of ADP-Glucose Pyrophosphorylase from Diverse Sources. J. Mol Evol. 34, 449-464.
28. Sowokinos, J.R. and Preiss, J. (1982) Pyrophosphorylases in Solanum tuberosum III. Purification, physical and catalytic properties of ADPglucose pyrophosphorylase in potatoes. Plant Physiol. 69, 1459-1466.
29. Stark, D.M., Timmerman, K.P., Barry, G.F., Preiss, J. and Kishore, G.M. (1992) Regulation of the amount of starch in plant tissues by ADP glucose pyrophosphorylase. Science, 258, 287-292.
30. Thorbjørnsen, T., Villand, P., Denyer, K., Olsen, O. and Smith, A.M. (1996) Distinct isoforms of ADPglucose pyrophosphorylase occur inside and outside the amyloplasts in barley endosperm Plant J. 10, 243-250.
31. Weber, H., Heim, U., Borisjuk, L. and Wobus, U. (1995) Cell-type specific, coordinate expression of two ADPglucose pyrophosphorylase genes in relation to starch biosynthesis during seed development in Vicia faba L. Planta, 195, 352-361.