Induction of genes encoding plastidic phosphorylase from spinach (Spinacia oleracea L.) and potato (Solanum tuberosum L.) by exogenously supplied carbohydrates in excised leaf discs

Planta

Volumn 203, Issue 1, 1997, Pages 111-120

  Duwenig, Elke ^a   Steup, Martin ^b   Kossmann, Jens ^c  

^a Institut fur Genbiologische Forschung Berlin GmbH   (Germany)

^b UNIVERSITY OF POTSDAM   (Germany)

^c MAX PLANCK INSTITUTE OF MOLECULAR PLANT PHYSIOLOGY   (Germany)

Author keywords

Gene expression (fruit enhanced, sugar induced); Plastidic phosphorylase (cDNA cloning, heterologous expression, expression analysis); Spinacia; Starch metabolism

Indexed keywords

CARBOHYDRATE; PHOSPHORYLASE; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BIOSYNTHESIS; CHEMISTRY; COMPARATIVE STUDY; DRUG EFFECT; ENZYME INDUCTION; ENZYMOLOGY; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; GENE LIBRARY; GENETIC TRANSCRIPTION; GENETICS; MOLECULAR CLONING; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PLANT LEAF; PLASTID; POTATO; SPINACH;

AMINO ACID SEQUENCE; CARBOHYDRATES; CLONING, MOLECULAR; ENZYME INDUCTION; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GENE EXPRESSION REGULATION, PLANT; GENE LIBRARY; MOLECULAR SEQUENCE DATA; PHOSPHORYLASES; PLANT LEAVES; PLASTIDS; RECOMBINANT PROTEINS; SOLANUM TUBEROSUM; SPINACIA OLERACEA; TRANSCRIPTION, GENETIC;

ANIMALIA; ESCHERICHIA COLI; PROKARYOTA; SOLANUM TUBEROSUM; SPINACIA; SPINACIA OLERACEA; TUBEROSUM;

EID: 0031239040     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004250050171     Document Type: Article

References (47)

1. Abel GJW, Springer F, Willmitzer L, Kossmann J (1996) Cloning and functional analysis of a cDNA encoding a novel 139 kDa starch synthase from potato (Solanum tuberosum L.). Plant J 10: 981-991
2. Amasino RM (1986) Acceleration of nucleic acid hybridisation rate by polyethylene glycol. Anal Biochem 152: 304-307
3. Bradford MM (1976) A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 243-254
4. Brisson N, Giroux H, Zollinger M, Camirand A, Simard C (1989) Maturation and subcellular compartmentation of potato starch phosphorylase. Plant Cell 1: 559-566
5. Browner MF, Fletterick RJ (1992) Phosphorylase: a biological transducer. TIBS 17: 66-71
6. Buchner P, Borisjuk L, Wobus U (1996) Glucan phosphorylases in Vicia faba L: cloning, structural analysis and expression patterns of cytosolic and plastidic forms in relation to starch. Planta 199: 64-73
7. Devereux J, Haeberli P, Smithies O (1984) A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 12: 387-395
8. Fukui T (1983) Plant phosphorylases. In: Akazawa T, Ashi T, Imaseki H (eds) The new frontiers in plant biochemistry. Japan Scientific Societies Press, Tokyo, pp 71-82
9. Giroux MJ, Boyer C, Feix G, Hannah LC (1994) Coordinated transcriptional regulation of storage product genes in the maize endosperm. Plant Physiol 106: 713-722
10. Greve B (1992) Immunochemische Analyse und submolekulare Charakterisierung pflanzlicher Heteropolymere mit Hilfe mono- und polyklonaler Antikörper. PhD thesis, Universität Münster, Germany
11. Hammond JBW, Preiss J (1983) Spinach leaf intra- and extrachloroplast phosphorylase activities during growth. Plant Physiol 73: 709-712
12. Ho LC (1988) Metabolism and compartmentation of imported sugars in sink organs in relation to sink strength. Annu Rev Plant Physiol Plant Mol Biol 39: 355-378
13. Jang J-C, Sheen J (1994) Sugar sensing in higher plants. Plant Cell 6: 1665-1679
14. Koch KE (1996) Carbohydrate-modulated gene expression in plants. Annu Rev Plant Physiol Plant Mol Biol 47: 509-540
15. Koch KE, Nolle KD, Duke ER, McCarty DR, Avigne WT (1992) Sugar levels modulate differential expression of maize sucrose synthase genes. Plant Cell 4: 56-69
16. Kossmann J (1992) Klonierung und funktioneile Analyse von Genen kodierend für am Kohlenhydratstoffwechsel der Kartoffel beteiligte Proteine. PhD thesis, Techn. Univ. Berlin
17. Kossmann J, Visser RGF, Müller-Röber BT, Willmitzer L, Sonnewald U (1991) Cloning and expression analysis of a potato cDNA that encodes branching enzyme: evidence for coexpression of starch biosynthetic genes. Mol Gen Genet 230: 39-44
18. Lin CT, Yeh K-W, Lee P-D, Su J-C (1990) Primary structure of sweet potato starch phosphorylase deduced from its cDNA sequence. Plant Physiol 95: 1250-1253
19. Logemann J, Schell J, Willmitzer L (1987) Improved method for the isolation of RNA from plant tissues. Anal Biochem 163: 21- 26
20. Mori H, Tanizawa K, Fukui T (1991) Potato tuber type H phosphorylase isozyme: molecular cloning nucleotide sequence and expression of a full-length cDNA in Escherichia coli. J Biol Chem 266: 18446-18453
21. Mori H, Tanizawa K, Fukui T (1993) A chimeric α-glucan phosphorylase of plant L and H isozyme: functional role of 78-residue insertion in type L isozyme. J Biol Chem 268: 5574- 5581
22. Müller-Röber B, Koßmann J, Hannah LC, Willmitzer L, Sonnewald U (1990) One of the two different ADP-glucose- pyrophosphorylase genes from potato responds strongly to elevated levels of sucrose. Mol Gen Genet 224: 136-146
23. Müller-Röber B, Sonnewald U, 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
24. Nakamura K, Ohto M, Yoshida N, Nakamura K (1991) Sucrose- induced accumulation of β-amylase occurs concomitant with the accumulation of starch and sporamin in leaf-petiole cuttings of the sweet potato. Plant Physiol 96: 902-909
25. Nakano K, Mori H, Fukui T (1989) Molecular cloning of cDNA encoding potato amyloplast α-glucan phosphorylase and the structure of its transit peptide. J Biochem 106: 691-695
26. Ohto M, Nakamura-Kito K, Nakamura K (1992) Induction of expression of genes coding for sporamin and β-amylase by polyglacturonic acid in leaf-petiole cuttings of sweet potato. Plant Physiol 99: 422-427
27. Palm D, Goerl R, Burger KJ (1985) Evolution of catalytic and regulatory sites in phosphorylases. Nature 313: 500-501
28. Pearson WR, Lipman DJ (1988) Improved tools for biological sequence comparison. Proc Natl Acad Sci USA 85: 2444-2448
29. Salanoubat M, Belliard G (1989) The steady-state level of potato sucrose synthase mRNA is dependent on wounding anaerobiosis and sucrose. Gene 84: 181-185
30. Sambrook J, Fritsch EF, Maniatis T (1989) Molecular cloning: a laboratory manual, 2nd edn. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, USA
31. Sanger F, Nicklen S, Coulson AR (1977) DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 74: 5463-5467
32. Schnarrenberger C (1990) Characterization and compartmentation, in green leaves, of hexokinases with different specificities for glucose, fructose, and mannose and for nucleoside triphosphate. Planta 181: 249-255
33. Schwartz. M (1966) Location of the maltose A and B loci on the genetic map of Escherichia coli. J Bact 92: 1083-1089
34. Shimomura S, Nagai M, Fukui T (1982) Comparative glucan specificities of two types of spinach leaf phosphorylase. J Biochem 91: 703-717
35. Smith AM, Martin C (1993) Starch biosynthesis and the potential for its manipulation. In: Grierson D (ed) Biosynthesis and manipulation of plant products: plant biotechnology series, vol 3. Blackie Academic and Professional, Glasgow, pp 1-54
36. Sonnewald U, Quick WP, Macrae E, Krause KP, Stitt M (1993) Purification, cloning and expression of spinach leaf sucrose- phosphate synthase in Escherichia coli. Planta 189: 174-181
37. Sonnewald U, Basner A, Greve B, Steup M (1995) A second L-type isozyme of potato glucan phosphorylase: cloning, antisense inhibition and expression analysis. Plant Mol Biol 27: 567-576
38. Stanley RG, Linskens HF (1974) Carbohydrates and cell walls. In: Stanley RG (ed) Pollen, Biology, biochemistry, management. Springer-Verlag, Heidelberg, pp 129-144
39. Steup M (1988) Starch degradation. In: Preiss J (ed) The biochemistry of plants, vol 14. Academic Press, London, pp 255-296
40. Steup M (1990) Starch degrading enzymes. In: Lea PJ (ed) Methods in plant biochemistry, vol 3, Academic Press, London, pp 103-128
41. St-Pierre B, Brisson N (1995) Induction of the plastidic starch phosphorylase gene in potato storage sink tissue. Effect of sucrose and evidence for coordinated regulation of phosphorylase and starch biosynthetic genes. Planta 95: 339-344
42. Titani K, Koide A, Hermann J, Ericsson LH, Mumar S, Wade RD, Walsh KA, Neurath H, Fischer EH (1977) Complete amino acid sequence of rabbit muscle glycogen phosphorylase. Proc Natl Acad Sci USA 74: 4762-4766
43. Turgeon TR (1989) The sink-source transition leaves. Annu Rev Plant Physiol Plant Mol Biol 40: 119-138
44. Van Berkel J, Conrads-Strauch J, Steup M (1991) Glucan-phosphorylase forms in cotyledons of Pisum sativum L.: localisation, developmental change, in vitro translation and processing. Planta 185: 432-439
45. Visser RGF, Stole A, Jacobsen AR (1991) Expression of a chimaeric granule-bound starch synthase-GUS gene in transgenic plants. Plant Mol Biol 17: 691-699
46. Von Schaewen A, Stitt M, Schmidt R, Sonnewald U, Willmitzer L (1990) Expression of yeast-derived invertase in the cell wall of tobacco and Arabidopsis plants leads to inhibition of sucrose export accumulation of carbohydrate and inhibition of photosynthesis and strongly influence growth and habitus of transgenic tobacco plants. EMBO J 9: 3033-3044
47. Yu F, Jen Y, Takeuchi E, Inouye M, Nakayama H, Tagaya M, Fukui T (1988) α-Glucan phosphorylase from Escherichia coli. J Biol Chem 263: 13706-13711