Skip to main content
Log in

Comparison of the primary sequences of two potato tuber ADP-glucose pyrophosphorylase subunits

  • Update Section
  • Short Communication
  • Published:
Plant Molecular Biology Aims and scope Submit manuscript

Abstract

Near-full-length cDNA clones to the small and large subunit of the heterotetrameric potato tuber ADP-glucose pyrophosphorylase have been isolated and characterized. The missing amino terminal sequence of the small subunit has also been elucidated from its corresponding genomic clone. Primary sequence comparisons revealed that each potato subunit had less identity to each other than to their homologous subunit from other plants. It also appeared that the smaller subunit is more conserved among the different plants and the larger subunit more divergent. Amino acid comparisons of both potato tuber sequences to theEscherichia coli ADP-glucose pyrophosphorylase sequence revealed conserved regions important for both catalytic and allosteric function of the bacterial enzyme.

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

Access this article

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

Instant access to the full article PDF.

Institutional subscriptions

References

  1. 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 

  2. Anderson JM, Okita TW, Preiss J: Enhancing carbon flow into starch: The role of ADP-glucose pyrophosphorylase. In: Vayda ME, Park WD (eds) The Molecular Biology of the Potato, pp. 159–180. C.A.B. International, Wallingford (1990).

    Google Scholar 

  3. Baecker PA, Furlong CE, Preiss J: Biosynthesis of bacterial glycogen: Primary structure ofEscherichia coli ADP-glucose synthetase as deduced from the nucleotide sequence of theglgC gene. J Biol Chem 258: 5084–5088 (1983).

    Google Scholar 

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

    Google Scholar 

  5. du Jardin P, Berhin A: Isolation and sequence analysis of a cDNA clone encoding a subunit of the ADP-glucose pyrophosphorylase of potato tuber amyloplasts. Plant Mol Biol 16: 349–351 (1991).

    Google Scholar 

  6. Heldt HW, Chon J, Maronde D, Stan Kovic ZS, Walker DA, Kraminer A, Kirk MR, Heber V: Role of orthophosphate and other factors in the regulation of starch formation in leaves and isolated chloroplasts. Plant Physiol 59: 1146–1155 (1977).

    Google Scholar 

  7. Kumar A, Ghosh P, Hill MA, Preiss J: Biosynthesis of bacterial glycogen: Determination of the amino acid changes that alter the regulatory properties of a mutantEscherichia coli ADP-glucose synthetase. J Biol Chem 264: 10464–10471 (1989).

    Google Scholar 

  8. Kumar A, Tanaka T, Lee YM, Preiss J: Biosynthesis of bacterial glycogen: Use of site-directed mutagenesis to probe the role of tyrosine114 in the catalytic mechanism of ADP-glucose synthetase fromEscherichia coli. J Biol Chem 263: 14634–14639 (1988).

    Google Scholar 

  9. Krishnan HB, Reeves CD, Okita TW: ADP-glucose pyrophosphorylase is encoded by different mRNA transcripts in leaf and endosperm of cereals. Plant Physiol 81: 642–645 (1986).

    Google Scholar 

  10. Lee YM, Kumar A, Preiss J: Amino acid sequence of anEscherichia coli ADP-glucose synthetase allosteric mutant as deduced from the DNA sequence of theglgC gene. Nucl Acids Res 15: 10603 (1987).

    Google Scholar 

  11. Lee YM, Preiss J: Covalent modification of substrate-binding sites ofEscherichia coli ADP-glucose synthetase: Isolation and structural characterization of 8-azido-ADP-glucose-incorporated peptides. J Biol Chem 261: 1058–1064 (1986).

    Google Scholar 

  12. Lin TP, Caspar T, Somerville C, Preiss J: A starch deficient mutant ofArabidopsis thaliana with low ADP-glucose pyrophosphorylase activity lacks one of the two subunits of the enzyme. Plant Physiol 88: 1175–1181 (1988).

    Google Scholar 

  13. Morell M, Bloom M, Preiss J: Affinity labeling of the allosteric activator site(s) of spinach leaf ADP-glucose pyrophosphorylase. J Biol Chem 263: 633–637 (1988).

    Google Scholar 

  14. Muller-Rober 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 

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

    Google Scholar 

  16. 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 

  17. Parsons TF, Preiss J: Biosynthesis of a bacterial glycogen: Isolation and characterization of the pyridoxal-P allosteric activator site and the ADP-glucose-protected pyridoxal-P binding site ofEscherichia coli B ADP-glucose synthase. J Biol Chem 253: 7638–7645 (1978).

    Google Scholar 

  18. Preiss J: Regulation of ADP-glucose pyrophosphorylase. In: Meister A (ed) Advances in Enzymology and Related Areas of Molecular Biology, vol 46, pp. 317–381. John Wiley, New York (1978).

    Google Scholar 

  19. Preiss J: Bacterial glycogen synthesis and its regulation. Annu Rev Microbiol 38: 419–458 (1984).

    Google Scholar 

  20. Preiss J: Biosynthesis of starch and its regulation. In: Preiss J (ed) The Biochemistry of Plants, vol 14: Carbohydrates, pp. 184–249. Academic Press, San Diego (1988).

    Google Scholar 

  21. Preiss J: Biochemistry and molecular biology of starch biosynthesis and its regulation. In: Miflin BJ (ed) Oxford Survey of Plant Molecular and Cellular Biology, vol 7. Oxford University Press, Oxford, in press.

  22. Preiss J, Ball K, Hutney J, Smith-White B, Li L, Okita TW: Regulatory mechanisms involved in the biosynthesis of starch. Pure Appl Chem 63: 535–544 (1991).

    Google Scholar 

  23. Preiss J, Cress D, Hutney J, Morell M, Bloom M, Okita T, Anderson J: Regulation of starch synthesis: Biochemical and genetic studies. In: Whitaker JR, Sonnet PE (eds) ACS Symposium Series 389 on Biocatalysis in Agricultural Biotechnology, pp. 84–92. American Chemical Society, Washington, DC (1989).

    Google Scholar 

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

    Google Scholar 

  25. Preiss J, Ghosh HP, Wittkop J: Regulation of the biosynthesis of starch in spinach chloroplast. In: Goodwin TW (ed) Biochemistry of Chloroplasts, vol 2, pp. 131–153. Academic Press, New York (1967).

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Nakata, P.A., Greene, T.W., Anderson, J.M. et al. Comparison of the primary sequences of two potato tuber ADP-glucose pyrophosphorylase subunits. Plant Mol Biol 17, 1089–1093 (1991). https://doi.org/10.1007/BF00037149

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00037149

Key words

Navigation