Skip to main content
SpringerLink
Log in

Molecular cloning and characterization of ADP-glucose pyrophosphorylase cDNA clones isolated from pea cotyledons

  • Published:
Plant Molecular Biology Aims and scope Submit manuscript

Abstract

Three ADP-glucose pyrophosphorylase (ADPG-PPase) cDNA clones have been isolated and characterized from a pea cotyledon cDNA library. Two of these clones (Psagps1 and Psagps2) encode the small subunit of ADPG-PPase. The deduced amino acid sequences for these two clones are 95% identical. Expression of these two genes differs in that the Psagps2 gene shows comparatively higher expression in seeds relative to its expression in other tissues. Psagps2 expression also peaks midway through seed development at a time in which Psagps1 transcripts are still accumulating. The third cDNA isolated (Psagpl1) encodes the large subunit of ADPG-PPase. It shows greater selectivity in expression than either of the small subunit clones. It is highly expressed in sink organs (seed, pod, and seed coat) and undetectable in leaves.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Ainsworth C, Tarvis M, Clark J: Isolation and analysis of a cDNA clone encoding the small subunit of ADP-glucose pyrophosphorylase from wheat. Plant Mol Biol 23: 23–33 (1993).

    Google Scholar 

  2. Anderson JM, Hnilo J, Larson R, Okita TW, Morell M, Preiss J: The encoded primary sequence of a rice seed ADP-glucose pyrophosphorylase subunit and its homology to the bacterial enzyme. J Biol Chem 264: 12238–12242 (1989).

    Google Scholar 

  3. Bae JM, Giroux M, Hannah L: Cloning and characterization of the Brittle-2 gene of maize. Maydica 35: 317–322 (1990).

    Google Scholar 

  4. Baecker PA, Furlong CE, Preiss J: Biosynthesis of bacterial glycogen: primary structure of Escherichia coli ADP glucose synthetase as deduced from the nucleotide sequence of the glgC gene. J Biol Chem 258: 5084–5088 (1983).

    Google Scholar 

  5. Ballicora MA, Laughlin MJ, Fu Y, Okita TW, Barry GF, Preiss J: Adenosine 50-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 (1995).

    Google Scholar 

  6. Bhattacharyya MK, Smith AM, Ellis THN, Hedley C, Martin C: The wrinkled-seed character of pea described by Mendel is caused by a transposon-like insertion in a gene encoding starch-branching enzyme. Cell 60: 115–122 (1990).

    Google Scholar 

  7. Bhave MR, Lawrence S, Barton C, Hannah LC: Identification and molecular characterization of Shrunken-2 cDNA clones of maize. Plant Cell 2: 581–588 (1990).

    Google Scholar 

  8. Burgess D, Taylor WC: Chloroplast photooxidation affects the accumulation of cytosolic mRNAs encoding chloroplast proteins in maize. Planta 170: 520–527 (1987).

    Google Scholar 

  9. Chen B-Y, Janes HW: ADP-Glc pyrophosphorylase small subunit cDNA from tomato fruit (accession no. L41126). Plant Physiol 109: 1498 (1995).

    Google Scholar 

  10. Denyer K, Foster J, Smith AM: The contributions of adenosine 5′-diphosphoglucose pyrophosphorylase and starch-branching enzyme to the control of starch synthesis in developing pea embryos. Planta 197: 57–62 (1995).

    Google Scholar 

  11. Foster JM, Smith AM: Metabolism of glucose 6-phosphate by plastids from developing pea embryos. Planta 190: 17–24 (1993).

    Google Scholar 

  12. Frohman MA: RACE: rapid amplification of cDNA ends. In: Innis MA, Gelfand DH, Sninsky JJ, White TJ (eds) PCR Protocols: A Guide to Methods and Applications, pp. 28–38. Academic Press, San Diego (1990).

    Google Scholar 

  13. Giroux M, Smith-White B, Gilmore V, Hannah LC, Preiss J: The large subunit of the embryo isoform of ADP glucose pyrophosphorylase from maize. Plant Physiol 108: 1333–1334 (1995).

    Google Scholar 

  14. Giroux MJ, Hannah LC: ADP-glucose pyrophosphorylase in shrunken-2 and brittle-2 mutants of maize. Mol Gen Genet 243: 400–408 (1994).

    Google Scholar 

  15. Gritton ET: Pea breeding. In: Bassett MJ(eds), Breeding Vegetable Crops, pp. 283–319. AVI Publishing Co., Westport, CT (1986).

    Google Scholar 

  16. Hannah LC, Giroux M, Boyer C: Biotechnological modification of carbohydrates for sweet corn and maize improvement. Sci Hort 55: 177–197 (1993).

    Google Scholar 

  17. Hanson KR, McHale NA: A starchless mutant of Nicotiana sylvestris containing a modified plastid phosphoglucomutase. Plant Physiol 88: 838–844 (1988).

    Google Scholar 

  18. Hill LM, Smith AM: Evidence that glucose 6-phosphate is imported as the substrate for starch synthesis by the plastids of developing pea embryos. Planta 185: 91–96 (1991).

    Google Scholar 

  19. Hylton C, Smith AM: The rb mutation of peas causes structural and regulatory changes in ADP glucose pyrophosphorylase from developing embryos. Plant Physiol 99: 1626–1634 (1992).

    Google Scholar 

  20. Jones JDG, Dunsmuir P, Bedbrook J: High level expression of introduced chimaeric genes in regenerated transformed plants. EMBO J 4: 2411–2418 (1985).

    Google Scholar 

  21. Joshi CP: An inspection of the domain between putative TATA box and translation start site in 79 plant genes. Nucl Acids Res 15: 6643–6653 (1987).

    Google Scholar 

  22. Keegstra K, Olsen LJ, Theg SM: Chloroplastic precursors and their transport across the envelope membranes. Annu Rev Plant Physiol Plant Mol Biol 40: 471–501 (1989).

    Google Scholar 

  23. Kim WT, Franceschi VR, Okita TW, Robinson NL, Morell M, Preiss J: Immunocytochemical localization of ADPglucose pyrophosphorylase in developing potato tuber cells. Plant Physiol 91: 217–220 (1989).

    Google Scholar 

  24. Kleczkowski LA, Villand P, Lthi E, Olsen O-A, Preiss J: Insensitivity of barley endosperm ADP-glucose pyrophosphorylase to 3-phosphoglycerate and orthophosphate regulation. Plant Physiol 101: 179–186 (1993).

    Google Scholar 

  25. Kozak M: Context effects and inefficient initiation at non-AUG codons in eukaryotic cell-free translation systems. Mol Cell Biol 9: 5073–5080 (1989).

    Google Scholar 

  26. La Cognata U, Willmitzer L, Müller-Röber B: Molecular cloning and characterization of novel isoforms of potato ADPglucose pyrophosphorylase. Mol Gen Genet 246: 538–548 (1995).

    Google Scholar 

  27. Malik AN, McLean PM, Roberts A, Barnett PS, Demaine AG, Banga JP, McGregor AM: A simple high yield method for the preparation of lambda gt10 DNA suitable for subcloning, amplification, and direct sequencing. Nucl Acids Res 18: 4031–4032 (1990).

    Google Scholar 

  28. Maniatis T, Fritsch EF, Sambrook J: Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratories, Cold Spring Harbor, NY (1982).

    Google Scholar 

  29. Maxam AM, Gilbert W: Sequencing end-labeled DNA with base-specific chemical cleavages. Meth Enzymol 65: 499–560 (1980).

    Google Scholar 

  30. Morell MK, Bloom M, Knowles V, Preiss J: Subunit structure of spinach leaf ADPglucose pyrophosphorylase. Plant Physiol 85: 182–187 (1987).

    Google Scholar 

  31. Müller-Röber B, Nast G, Willmitzer L: Isolation and expression analysis of cDNA clones encoding a small and a large subunit of ADP-glucose pyrophosphorylase from sugar beet. Plant Mol Biol 27: 191–197 (1995).

    Google Scholar 

  32. Müller-Röber BT, Kossmann J, Hannah LC, Willmitzer L, Sonnewald U: One of two different ADP-glucose pyrophosphorylase genes from potato responds strongly to elevated levels of sucrose. Mol Gen Genet 224: 136–146 (1990).

    Google Scholar 

  33. Nakata PA, Greene TW, Anderson JM, Smith-White BJ, Okita TW, Preiss J: Comparison of the primary sequences of two potato tuber ADP-glucose pyrophosphorylase subunits. Plant Mol Biol 17: 1089–1093 (1991).

    Google Scholar 

  34. Okita TW, Nakata PA, Anderson JM, Sowokinos J, Morell M, Preiss J: The subunit structure of potato tuber ADPglucose pyrophosphorylase. Plant Physiol 93: 785–790 (1990).

    Google Scholar 

  35. Olive MR, Ellis RJ, Schuch WW: Isolation and nucleotide sequences of cDNA clones encoding ADP-glucose pyrophosphorylase polypeptides from wheat leaf and endosperm. Plant Mol Biol 12: 525–538 (1989).

    Google Scholar 

  36. Pate JS, Flinn AM: Fruit and seed development. In: Sutcliffe JF, Pate JS (eds) The Physiology of the Garden Pea, pp. 431–468. Academic Press, San Francisco (1977).

    Google Scholar 

  37. Plaxton WC, Preiss J: Purification and properties of nonproteolytic degraded ADPglucose pyrophosphorylase from maize endosperm. Plant Physiol 83: 105–112 (1987).

    Google Scholar 

  38. Pozueta-Romero J, Frehner M, Viale AM, Akazawa T: Direct transport of ADPglucose by an adenylate translocator is linked to starch biosynthesis in amyloplasts. Proc Natl Acad Sci USA 88: 5769–5773 (1991).

    Google Scholar 

  39. Preiss J: Biology and molecular biology of starch synthesis and regulation. Oxford Surv Plant Mol Cell Biol 7: 59–114 (1991).

    Google Scholar 

  40. Preiss J: Biosynthesis of starch and its regulation. In: Loewus FA, Tanner W (eds) Encyclopedia of Plant Physiology, New Series, pp. 397–417. Springer-Verlag, New York (1982).

    Google Scholar 

  41. Preiss J, Bloom M, Morell M, Knowles VL, Plaxton WC, Okita TW, Larsen R, Harmon AC, Putnam-Evans C: Regulation of starch synthesis: enzymological and genetic studies. In: Bruening G, Harada J, Kosuge T, Hollaender A(eds) Tailoring Genes for Crop Improvement, pp. 133–152. Plenum Press, New York (1987).

    Google Scholar 

  42. Preiss J, Danner S, Summers PS, Morell M, Barton CR, Yang L, Nieder M: Molecular characterization of the Brittle-2 gene effect on maize endosperm ADPglucose pyrophosphorylase subunits. Plant Physiol 92: 881–885 (1990).

    Google Scholar 

  43. Prioul J-L, Jeannette E, Reyss A, Gregory N, Giroux M, Hannah LC, Causse M: Expression of ADP-glucose pyrophosphorylase in maize (Zea mays L.) grain and source leaf during grain filling. Plant Physiol 104: 179–187 (1994).

    Google Scholar 

  44. Rochat C, Boutin J-P: Temporary storage compounds and sucrose-starch metabolism in seed coats during pea seed development (Pisum sativum). Physiol Plant 85: 567–572 (1992).

    Google Scholar 

  45. Smith AM, Denyer K: Tansley review No. 39: Starch synthesis in developing pea embryos. New Phytol 122: 21–33 (1992).

    Google Scholar 

  46. Smith AM, Quinton-Tulloch J, Denyer K: Characteristics of plastids responsible for starch synthesis in developing pea embryos. Planta 180: 517–523 (1990).

    Google Scholar 

  47. Smith-White BJ, Preiss J: Comparison of proteins of ADPglucose pyrophosphorylase from diverse sources. J Mol Evol 34: 449–464 (1992).

    Google Scholar 

  48. Stark DM, Timmerman KP, Barry GF, Preiss J, Kishore GM: Regulation of the amount of starch in plant tissues by ADP glucose pyrophosphorylase. Science 258: 287–292 (1992).

    Google Scholar 

  49. Taylor JL, Jones JDG, Sandler S, Mueller GM, Bedbrook J, Dunsmuir P: Optimizing the expression of chimeric genes in plant cells. Mol Gen Genet 210: 572–577 (1987).

    Google Scholar 

  50. Thorbjørnsen T, Villand P, Denyer K, Olsen O-A, Smith AM: Distinct isoforms of ADPglucose pyrophosphorylase occur inside and outside the amyloplasts in barley endosperm. Plant J 10: 243–250 (1996).

    Google Scholar 

  51. Thorbjørnsen T, Villand P, Kleczkowski LA, Olsen O-A: A single gene encodes two different transcripts for the ADP-glucose pyrophosphorylase small subunit from barley (Hordeum vulgare). Biochem J 313: 149–154 (1996).

    Google Scholar 

  52. Turgeon R: The sink-source transition in leaves. Annu Rev Plant Physiol Plant Mol Biol 40: 119–138 (1989).

    Google Scholar 

  53. Villand P, Aalen R, Olsen O-A, Lüthi E, Lönneborg A, Kleczkowski LA: PCR amplification and sequences of cDNA clones for the small and large subunits of ADP-glucose pyrophosphorylase from barley tissues. Plant Mol Biol 19: 381–389 (1992).

    Google Scholar 

  54. Villand P, Kleczkowski LA: Is there an alternative pathway for starch biosynthesis in cereal seeds? Z Naturforsch 49c: 215–219 (1994).

    Google Scholar 

  55. Villand P, Olsen O-A, Kilian A, Kleczkowski LA: ADPglucose pyrophosphorylase large subunit cDNA from barley endosperm. Plant Physiol 100: 1617–1618 (1992).

    Google Scholar 

  56. Villand P, Olsen O-A, Kleczkowski LA: Molecular characterization of multiple cDNA clones for ADP-glucose pyrophosphorylase from Arabidopsis thaliana. Plant Mol Biol 23: 1279–1284 (1993).

    Google Scholar 

  57. Weber H, Heim U, Borisjuk L, Wobus U: Cell-type specific, coordinate expression of two ADP-glucose pyrophosphorylase genes in relation to starch biosynthesis during seed development of Vicia faba L. Planta 195: 352–361 (1995).

    Google Scholar 

  58. Wood WI: Gene cloning based on long oligonucleotide probes. Meth Enzymol 152: 443–447 (1987).

    Google Scholar 

Download references

Author information

Author notes

  1. Andrea Penton

    Present address: McArdle Laboratories, 1400 University Ave., Madison, WI, 53706, USA

  2. Hugo Dooner

    Present address: The Waksman Institute, Rutgers University, Piscataway, NJ, 08855, USA

Authors and Affiliations

  1. DNA Plant Technology Corporation, 6701 San Pablo Ave., Oakland, CA, 94608, USA

    Diane Burgess, Andrea Penton, Pamela Dunsmuir & Hugo Dooner

Authors
  1. Diane Burgess
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Andrea Penton
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Pamela Dunsmuir
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Hugo Dooner
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Burgess, D., Penton, A., Dunsmuir, P. et al. Molecular cloning and characterization of ADP-glucose pyrophosphorylase cDNA clones isolated from pea cotyledons. Plant Mol Biol 33, 431–444 (1997). https://doi.org/10.1023/A:1005752311130

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1005752311130

Search

Navigation