ArticlePlant physiology2008
Starch biosynthetic enzymes from developing maize endosperm associate in multisubunit complexes.
Article in Plant physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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Who cites it
91 citing papers in PubMed, 214 citations in OpenAlex.
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- Starch Synthase 3 isoforms are essential for normal starch granule initiation in wheat endosperm.The New phytologist · 2026Article
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- The bHLH transcription factor PIL1 orchestrates starch synthesis in key cereal crops.Nature communications · 2025Article
- Noncatalytic functions of ISOAMYLASE 1 and 2 affect the proportion of insoluble and soluble α-polyglucans in maize.The Plant cell · 2025Article
- Interactions of separately conserved α-(1→6) glucosidases that participate in maize endosperm starch biosynthesis.Plant physiology · 2025Article
- Covalently linked phosphate monoesters on alpha-polyglucans reduce substrate affinity of branching enzymes.Carbohydrate polymers · 2025Article
- Triple gene mutations boost amylose and resistant starch content in rice: insights fromFrontiers in plant science · 2024Article
- Soluble and insoluble α-glucan synthesis in yeast by enzyme suites derived exclusively from maize endosperm.Plant physiology · 2023Article
- FLOURY ENDOSPERM 6 mutations enhance the sugary phenotype caused by the loss of ISOAMYLASE1 in barley.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2023Article
- Nitrogen-dependent binding of the transcription factor PBF1 contributes to the balance of protein and carbohydrate storage in maize endosperm.The Plant cell · 2023Article
- BE3 is the major branching enzyme isoform required for amylopectin synthesis in CFrontiers in plant science · 2023Article
- Genome-Wide Identification of DOF Gene Family and the Mechanism Dissection ofInternational journal of molecular sciences · 2022Article
- Dynamic Change in Starch Biosynthetic Enzymes Complexes during Grain-Filling Stages in BEIIb Active and Deficient Rice.International journal of molecular sciences · 2022Article
- A Maize CBM Domain Containing the Protein ZmCBM48-1 Positively Regulates Starch Synthesis in the Rice Endosperm.International journal of molecular sciences · 2022Article
- Maize RNA 3'-terminal phosphate cyclase-like protein promotes 18S pre-rRNA cleavage and is important for kernel development.The Plant cell · 2022Article
- Pleiotropic ZmICE1 Is an Important Transcriptional Regulator of Maize Endosperm Starch Biosynthesis.Frontiers in plant science · 2022Article
- Starch Biosynthetic Protein Complex Formation in RiceJournal of applied glycoscience · 2022Article
- Coalescence and directed anisotropic growth of starch granule initials in subdomains of Arabidopsis thaliana chloroplasts.Nature communications · 2021Article
31 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mutations affecting specific starch biosynthetic enzymes commonly have pleiotropic effects on other enzymes in the same metabolic pathway. Such genetic evidence indicates functional relationships between components of the starch biosynthetic system, including starch synthases (SSs), starch branching enzymes (BEs), and starch debranching enzymes; however, the molecular explanation for these functional interactions is not known. One possibility is that specific SSs, BEs, and/or starch debranching enzymes associate physically with each other in multisubunit complexes. To test this hypothesis, this study sought to identify stable associations between three separate SS polypeptides (SSI, SSIIa, and SSIII) and three separate BE polypeptides (BEI, BEIIa, and BEIIb) from maize (Zea mays) amyloplasts. Detection methods included in vivo protein-protein interaction tests in yeast (Saccharomyces cerevisiae) nuclei, immunoprecipitation, and affinity purification using recombinant proteins as the solid phase ligand. Eight different instances were detected of specific pairs of proteins associating either directly or indirectly in the same multisubunit complex, and direct, pairwise interactions were indicated by the in vivo test in yeast. In addition, SSIIa, SSIII, BEIIa, and BEIIb all comigrated in gel permeation chromatography in a high molecular mass form of approximately 600 kD, and SSIIa, BEIIa, and BEIIb also migrated in a second high molecular form, lacking SSIII, of approximately 300 kD. Monomer forms of all four proteins were also detected by gel permeation chromatography. The 600- and 300-kD complexes were stable at high salt concentration, suggesting that hydrophobic effects are involved in the association between subunits.
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