Abstract
A cDNA clone (WL : AGA.1) encoding wheat leaf ADP-glucose pyrophosphorylase has been isolated from a λgt11 expression library, by immunological screening with anti-spinach leaf ADP-glucose pyrophosphorylase serum. The WL : AGA.1 cDNA is 948 bp long and contains approximately 55% of the complete wheat leaf ADP-glucose pyrophosphorylase mRNA sequence, estimated from Northern blot experiments. A wheat endosperm cDNA library was subsequently constructed in λgt11 and six clones hybridising to the cDNA insert of clone WL : AGA.1 were isolated. The longest of these wheat endosperm ADP-glucose pyrophosphorylase cDNAs, clone WE : AGA.7, is nearly full-length (1798 bp), indicated by Northern blot analysis of wheat endosperm mRNA and nucleotide sequence analysis.
Southern hybridisation analysis and restriction enzyme map** indicated that the wheat leaf and wheat endosperm ADP-glucose pyrophosphorylase cDNAs and genes are members of two distinct gene families. In addition, restriction enzyme map** revealed polymorphism in the wheat endosperm ADP-glucose pyrophosphorylase cDNAs, indicating the existence of at least two wheat endosperm ADP-glucose pyrophosphorylase gene sub-families.
Subsequent nucleotide sequence analysis indicates that there is approximately 55% identity between wheat leaf and wheat endosperm ADP-glucose pyrophosphorylase cDNAs. In contrast, members of each sub-family of endosperm cDNA, represented by clones WE : AGA.3 and WE : AGA.7, are 96% identical.
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Aviv H, Leder P: Purification of biologically active globin messenger RNA by chromatography on oligothymidilic acid-cellulose. Proc Natl Acad Sci 69: 1408–1412 (1972).
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).
Birnboim HC, Doly J: A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucl Acids Res 7: 1513–1523 (1779).
Chou PY, Fasman GD: Prediction of the secondary structure of proteins from their amino acid sequence. Adv Enzymol 47: 45–147 (1978).
Copeland L, Preiss J: Purification of spinach leaf ADP-glucose pyrophosphorylase. Plant Physiol 68: 996–1001 (1981).
Entwhistle G, Tyson RH, ap Rees T: Isolation of amyloplasts from wheat endosperm. Phytochemistry 27: 993–996 (1988).
Espada J: Enzymic synthesis of adenosine diphosphate glucose from glucose-1-phosphate and adenosine triphosphate. J Biol Chem 237: 3577–3581 (1962).
Greene FC:In vitro synthesis of wheat (Triticum aestivum L.) storage proteins. Plant Physiol 68: 778–783 (1981).
Gubler U, Hoffman BJ: A simple and very efficient method for generating complementary DNA libraries. Gene 25: 263–270 (1983).
Heldt HW, Rapley L: Specific transport of inorganic phosphate, 3-phosphoglycerate and dihydroxacetone phosphate, and of dicarboxylates across the inner membrane of spinach chloroplasts. FEBS Lett 10: 143–148 (1970).
Hollemans M, Runswick MJ, Fearnley IM, Walker JE: The sites of labeling of the beta subunit of bovine mitochondrial F-1 ATPase with 8 azido ATP. J Biol Chem 258: 9307–9313 (1983).
Huynh TV, Young RA, Davis RW: Construction and screening of cDNA libraries in λgt10 and λgt11. In: Glover D (ed) DNA Cloning, vol I: A Practical Approach, pp. 49–78. IRL Press, Oxford (1980).
Jansen T, Rother C, Steppuhn J, Reinke H, Beyreuther K, Jansson C, Andersson B, Herrmann RG: Nucleotide sequence of cDNA clones encoding the complete 23 kDa and 16 kDa precursor proteins associated with the photosynthetic oxygen-evolving complex from spinach. FEBS Lett 216: 234–240 (1987).
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).
Joshi CP: Putative polyadenylation signals in nuclear genes of higher plants: A compilation and analysis. Nucl Acids Res 15: 9627–9639 (1987).
Kaiser WM, Bassham JA: Light-dark regulation of starch metabolism in chloroplasts I: Levels of metabolites in chloroplasts and medium during light-dark transition. Plant Physiol 63: 105–108 (1979).
Kaiser WM, Bassham JA: Light-dark regulation of starch metabolism in chloroplasts II: Effect of chloroplastic metabolite levels on the formation of ADP-glucose by chloroplast extracts. Plant Physiol 63: 109–113 (1979).
Keeling PL, Wood JR, Tyson H, Bridges IG: Starch biosynthesis in the develo** wheat grain. Plant Physiol 87: 311–319 (1988).
Kerlavage AR, Taylor SS: Govalent modification of a cyclic AMP binding site of the regulatory subunit of cyclic AMP dependent protein kinase II EC-2.7.1.37 with 8-azido cyclic AMP: Identification of a single modified tyrosine residue. J Biol Chem 255: 8483–4888 (1980).
Klösgen RB, Gierl A, Schwarz-Sommer Z, Saedler H: Molecular analysis of thewaxy locus ofZea mays. Mol Gen Genet 203: 237–244 (1986).
Kozak M: Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell 44: 283–292 (1986).
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).
Lee Y-M, Preiss J: Covalent modification of substratebinding sites ofEscherichia coli ADP-glucose synthetase: Isolation and structural characterisation of 8-azido-ADP-glucose incorporated peptides. J Biol Chem 261: 1058–1064 (1986).
MacDonald PW, Strobel GA: Adenosine diphosphate glucose pyrophosphorylase control of starch accumulation in rust-infected wheat leaves. Plant Physiol 46: 126–135 (1970).
Maniatis T, Fritsch EF, Sambrook J: Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY (1982).
Mazur BJ, Chui C-F: Sequence of a genomic DNA clone for the small subunit of ribulose bisphosphate carboxylase-oxygenase from tobacco. Nucl Acids Res 13: 2373–2386 (1985).
Murray MG, Thompson WF: Rapid isolation of high molecular weight plant DNA. Nucl Acids Res 8: 4321–4325 (1980).
Olive MR: Wheat starch biosynthesis: Organ-specific expression of genes encoding ADP-glucose pyrophosphorylase. PhD Thesis, Dept of Biological Sciences, University of Warwick, Coventry, UK (1988).
Pai EF, Sachsenheimer W, Schirmer RH, Schulz GE: Substrate positions and induced fit in crystalline adenylate kinase. J Mol Biol 114: 37–46 (1977).
Parsons TF, Preiss J: Biosynthesis of bacterial glycogen: Incorporation of pyridoxal phosphate into the allosteric activator site of an ADP-glucose-protected pyridoxal phosphate-binding site ofEscherichia coli B ADP-glucose synthase, J Biol Chem 253: 6197–6202 (1978).
Parsons TF, Preiss J: Biosynthesis of bacterial glycogen: Isolation and characterisation 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).
Preiss J, Bloom M, Morell M, Knowles V, Plaxton WC, Okita TW, Larsen R, Harmon AC, Putnam-Evans C: Regulation of starch synthesis: Enzymological and genetic studies. In: Bruening G, Harada J, Kosuga T, Hollaender A (eds), Tailoring Genes for Crop Improvement—An Agricultural Perspective, pp. 133–152. Plenum Press, New York (1987).
Recondo E, Leloir LF: Adenosine diphosphate glucose and starch synthesis. Biochem Biophys Res Comm 6: 85–88 (1961).
Sanger F, Nicklen S, Coulson AR: DNA sequencing with chain terminating inhibitors. Proc Natl Acad Sci USA 74: 5463–5467 (1977).
Sanwal GG, Greenberg E, Hardie J, Cameron EC, Preiss J: Regulation of starch biosynthesis in plant leaves: Activation and inhibition of ADP-glucose pyrophosphorylase. Plant Physiol 43: 417–427 (1968).
Schmidt GW, Mishkind ML: The transport of proteins into chloroplasts. Ann Rev Biochem 55: 879–912 (1986).
Spilatro SR, Preiss J: Regulation of starch synthesis in the bundle sheath and mesophyll ofZea mays L.: Intercellular compartmentalisation of enzymes of starch metabolism and the properties of the ADP-glucose pyrophosphorylases. Plant Physiol 83: 621–627 (1987).
Staden R: Automation of the computer handling of gel reading data produced by the shotgun method of DNA sequencing. Nucl Acids Res 10: 4731–4751 (1982).
Steup M, Peavey DG, Gibbs M: The regulation of starch metabolism by inorganic phosphate. Biochem Biophys Res Comm 72: 1554–1561 (1976).
Tyson RH, ap Rees T: Starch biosynthesis by isolated amyloplasts from wheat endosperm. Planta, in press.
Young RA, Davis RW: Efficient isolation of genes by using antibody probes. Proc Natl Acad Sci USA 80: 1194–1198 (1983).
Young RA, Davis RW: Yeast RNA polymerase II genes: Isolation with antibody probes. Science 222: 778–782 (1983).
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Olive, M.R., Ellis, R.J. & Schuch, W.W. Isolation and nucleotide sequences of cDNA clones encoding ADP-glucose pyrophosphorylase polypeptides from wheat leaf and endosperm. Plant Mol Biol 12, 525–538 (1989). https://doi.org/10.1007/BF00036967
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DOI: https://doi.org/10.1007/BF00036967