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. 1995 Apr;7(4):417–429. doi: 10.1105/tpc.7.4.417

Characterization of the maize gene sugary1, a determinant of starch composition in kernels.

M G James 1, D S Robertson 1, A M Myers 1
PMCID: PMC160793  PMID: 7773016

Abstract

In maize kernels, mutations in the gene sugary1 (su1) result in (1) increased sucrose concentration; (2) decreased concentration of amylopectin, the branched component of starch; and (3) accumulation of the highly branched glucopolysaccharide phytoglycogen. To investigate further the mechanisms of storage carbohydrate synthesis in maize, part of the su1 gene locus and a cDNA copy of the su1 transcript were characterized. Five new su1 mutations were isolated in a Mutator background, and the mutant allele su1-R4582::Mu1 was isolated by transposon tagging. The identity of the cloned element as the su1 gene locus was confirmed by the cosegregation of restriction fragment length polymorphisms in the same or nearby genomic intervals with three additional, independent su1 mutations. Pedigree analysis was also used to confirm the identity of su1. A 2.8-kb mRNA that is homologous to the cloned gene was detected in maize kernels, and a 2.7-kb cDNA clone was isolated based on hybridization to the genomic DNA. Specific portions of the cDNA hybridized with multiple segments of the maize genome, suggesting that su1 is part of a multigene family. The cDNA sequence specified a polypeptide of at least 742 amino acids, which is highly similar in amino acid sequence to bacterial enzymes that hydrolyze alpha-(1-->6) glucosyl linkages of starch. Therefore, debranching of glucopolysaccharides is seemingly part of the normal process of starch biosynthesis, and the final degree of branch linkages in starch most likely arises from the combined actions of branching and debranching enzymes.

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Selected References

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  1. Altschul S. F., Gish W., Miller W., Myers E. W., Lipman D. J. Basic local alignment search tool. J Mol Biol. 1990 Oct 5;215(3):403–410. doi: 10.1016/S0022-2836(05)80360-2. [DOI] [PubMed] [Google Scholar]
  2. Amemura A., Chakraborty R., Fujita M., Noumi T., Futai M. Cloning and nucleotide sequence of the isoamylase gene from Pseudomonas amyloderamosa SB-15. J Biol Chem. 1988 Jul 5;263(19):9271–9275. [PubMed] [Google Scholar]
  3. Barker R. F., Thompson D. V., Talbot D. R., Swanson J., Bennetzen J. L. Nucleotide sequence of the maize transposable element Mul. Nucleic Acids Res. 1984 Aug 10;12(15):5955–5967. doi: 10.1093/nar/12.15.5955. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Black R. C., Loerch J. D., McArdle F. J., Creech R. G. Genetic interactions affecting maize phytoglycogen and the phytoglycogen-forming branching enzyme. Genetics. 1966 Apr;53(4):661–668. doi: 10.1093/genetics/53.4.661. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Boyer C. D., Preiss J. Properties of Citrate-stimulated Starch Synthesis Catalyzed by Starch Synthase I of Developing Maize Kernels. Plant Physiol. 1979 Dec;64(6):1039–1042. doi: 10.1104/pp.64.6.1039. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Creech R G. Genetic Control of Carbohydrate Synthesis in Maize Endosperm. Genetics. 1965 Dec;52(6):1175–1186. doi: 10.1093/genetics/52.6.1175. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. ERLANDER S. R. A proposed mechanism for the synthesis of starch from glycogen. Enzymologia. 1958 Jun 30;19(5):273–283. [PubMed] [Google Scholar]
  8. Harada T., Misaki A., Akai H., Yokobayashi K., Sugimoto K. Characterization of Pseudomonas isoamylase by its actions on amylopectin and glycogen: comparison with Aerobacter pullulanase. Biochim Biophys Acta. 1972 May 12;268(2):497–505. doi: 10.1016/0005-2744(72)90345-2. [DOI] [PubMed] [Google Scholar]
  9. Jespersen H. M., MacGregor E. A., Henrissat B., Sierks M. R., Svensson B. Starch- and glycogen-debranching and branching enzymes: prediction of structural features of the catalytic (beta/alpha)8-barrel domain and evolutionary relationship to other amylolytic enzymes. J Protein Chem. 1993 Dec;12(6):791–805. doi: 10.1007/BF01024938. [DOI] [PubMed] [Google Scholar]
  10. Kainuma K., Kobayashi S., Harada T. Action of Pseudomonas isoamylase on various branched oligo and poly-saccharides. Carbohydr Res. 1978 Mar;61:345–357. doi: 10.1016/s0008-6215(00)84494-8. [DOI] [PubMed] [Google Scholar]
  11. Lee E. Y., Marshall J. J., Whelan W. J. The substrate specificity of amylopectin-debranching enzymes from sweet corn. Arch Biochem Biophys. 1971 Apr;143(2):365–374. doi: 10.1016/0003-9861(71)90223-2. [DOI] [PubMed] [Google Scholar]
  12. Lomako J., Lomako W. M., Whelan W. J. The substrate specificity of isoamylase and the preparation of apo-glycogenin. Carbohydr Res. 1992 Apr 6;227:331–338. doi: 10.1016/0008-6215(92)85082-b. [DOI] [PubMed] [Google Scholar]
  13. Lopes M. A., Larkins B. A. Endosperm origin, development, and function. Plant Cell. 1993 Oct;5(10):1383–1399. doi: 10.1105/tpc.5.10.1383. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. MacGregor E. A., Svensson B. A super-secondary structure predicted to be common to several alpha-1,4-D-glucan-cleaving enzymes. Biochem J. 1989 Apr 1;259(1):145–152. doi: 10.1042/bj2590145. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Macdonald F. D., Preiss J. Partial purification and characterization of granule-bound starch synthases from normal and waxy maize. Plant Physiol. 1985 Aug;78(4):849–852. doi: 10.1104/pp.78.4.849. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Mangelsdorf P. C. The Inheritance of Amylaceous Sugary Endosperm and Its Derivatives in Maize. Genetics. 1947 Sep;32(5):448–458. doi: 10.1093/genetics/32.5.448. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Matsuura Y., Kusunoki M., Harada W., Kakudo M. Structure and possible catalytic residues of Taka-amylase A. J Biochem. 1984 Mar;95(3):697–702. doi: 10.1093/oxfordjournals.jbchem.a134659. [DOI] [PubMed] [Google Scholar]
  18. NELSON O. E., RINES H. W. The enzymatic deficiency in the waxy mutant of maize. Biochem Biophys Res Commun. 1962 Oct 31;9:297–300. doi: 10.1016/0006-291x(62)90043-8. [DOI] [PubMed] [Google Scholar]
  19. Pan D., Nelson O. E. A debranching enzyme deficiency in endosperms of the sugary-1 mutants of maize. Plant Physiol. 1984 Feb;74(2):324–328. doi: 10.1104/pp.74.2.324. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Romeo T., Kumar A., Preiss J. Analysis of the Escherichia coli glycogen gene cluster suggests that catabolic enzymes are encoded among the biosynthetic genes. Gene. 1988 Oct 30;70(2):363–376. doi: 10.1016/0378-1119(88)90208-9. [DOI] [PubMed] [Google Scholar]
  21. Scanlon M. J., Stinard P. S., James M. G., Myers A. M., Robertson D. S. Genetic analysis of 63 mutations affecting maize kernel development isolated from Mutator stocks. Genetics. 1994 Jan;136(1):281–294. doi: 10.1093/genetics/136.1.281. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Shure M., Wessler S., Fedoroff N. Molecular identification and isolation of the Waxy locus in maize. Cell. 1983 Nov;35(1):225–233. doi: 10.1016/0092-8674(83)90225-8. [DOI] [PubMed] [Google Scholar]
  23. Singh B. K., Preiss J. Starch Branching Enzymes from Maize : Immunological Characterization using Polyclonal and Monoclonal Antibodies. Plant Physiol. 1985 Sep;79(1):34–40. doi: 10.1104/pp.79.1.34. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Stinard P. S., Robertson D. S., Schnable P. S. Genetic Isolation, Cloning, and Analysis of a Mutator-Induced, Dominant Antimorph of the Maize amylose extender1 Locus. Plant Cell. 1993 Nov;5(11):1555–1566. doi: 10.1105/tpc.5.11.1555. [DOI] [PMC free article] [PubMed] [Google Scholar]

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