ArticlePlant physiology2012
Functional interactions between starch synthase III and isoamylase-type starch-debranching enzyme in maize endosperm.
Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- Whole-Genome Resequencing ofInternational journal of molecular sciences · 2026Article
- Article
- Comparative analysis of starch structure and multi-omics profiles reveals candidate pathways associated with a novel soft-waxy maize trait.Frontiers in plant science · 2026Article
- Noncatalytic functions of ISOAMYLASE 1 and 2 affect the proportion of insoluble and soluble α-polyglucans in maize.The Plant cell · 2025Article
- Amylopectin branch trimming and biosynthesis elucidated by the rice isoamylase ISA1-ISA2 heterocomplex.Nature communications · 2025Article
- Comparison of Nutritional Quality and Functional Active Substances in Different Parts of Eight Lotus Seed Cultivars.Foods (Basel, Switzerland) · 2024Article
- Down-Regulation of Rice Glutelin byInternational journal of molecular sciences · 2023Article
- Comparative Phosphoproteomic Analysis Reveals the Response of Starch Metabolism to High-Temperature Stress in Rice Endosperm.International journal of molecular sciences · 2021Article
- Starch biosynthesis in cereal endosperms: An updated review over the last decade.Plant communications · 2021Review
- Allelic variation in sugary1 gene affecting kernel sweetness among diverse-mutant and -wild-type maize inbreds.Molecular genetics and genomics : MGG · 2021Article
- Posttranslational Modification of Waxy to Genetically Improve Starch Quality in Rice Grain.International journal of molecular sciences · 2021Review
- Starch and Glycogen Analyses: Methods and Techniques.Biomolecules · 2020Review
- A New SNP in Rice Gene Encoding Pyruvate Phosphate Dikinase (PPDK) Associated with Floury Endosperm.Genes · 2020Article
- Intra-Sample Heterogeneity of Potato Starch Reveals Fluctuation of Starch-Binding Proteins According to Granule Morphology.Plants (Basel, Switzerland) · 2019Article
- MaizeThe Journal of cell biology · 2019Article
- The DOF-Domain Transcription Factor ZmDOF36 Positively Regulates Starch Synthesis in Transgenic Maize.Frontiers in plant science · 2019Article
- Starch formation inside plastids of higher plants.Protoplasma · 2018Review
- Carbohydrate reserves and seed development: an overview.Plant reproduction · 2018Review
- Evolutionary, structural and expression analysis of core genes involved in starch synthesis.Scientific reports · 2018Article
- Functions of maize genes encoding pyruvate phosphate dikinase in developing endosperm.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
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9 authors.
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Abstract
This study characterized genetic interactions between the maize (Zea mays) genes dull1 (du1), encoding starch synthase III (SSIII), and isa2, encoding a noncatalytic subunit of heteromeric isoamylase-type starch-debranching enzyme (ISA1/ISA2 heteromer). Mutants lacking ISA2 still possess the ISA1 homomeric enzyme. Eight du1(-) mutations were characterized, and structural changes in amylopectin resulting from each were measured. In every instance, the same complex pattern of alterations in discontinuous spans of chain lengths was observed, which cannot be explained solely by a discrete range of substrates preferred by SSIII. Homozygous double mutants were constructed containing the null mutation isa2-339 and either du1-Ref, encoding a truncated SSIII protein lacking the catalytic domain, or the null allele du1-R4059. In contrast to the single mutant parents, double mutant endosperms affected in both SSIII and ISA2 were starch deficient and accumulated phytoglycogen. This phenotype was previously observed only in maize sugary1 mutants impaired for the catalytic subunit ISA1. ISA1 homomeric enzyme complexes assembled in both double mutants and were enzymatically active in vitro. Thus, SSIII is required for normal starch crystallization and the prevention of phytoglycogen accumulation when the only isoamylase-type debranching activity present is ISA1 homomer, but not in the wild-type condition, when both ISA1 homomer and ISA1/ISA2 heteromer are present. Previous genetic and biochemical analyses showed that SSIII also is required for normal glucan accumulation when the only isoamylase-type debranching enzyme activity present is ISA1/ISA heteromer. These data indicate that isoamylase-type debranching enzyme and SSIII work in a coordinated fashion to repress phytoglycogen accumulation.
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