ArticlePlant physiology2009
Proteins from multiple metabolic pathways associate with starch biosynthetic enzymes in high molecular weight complexes: a model for regulation of carbon allocation in maize amyloplasts.
Article in Plant physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.
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Who cites it
88 citing papers in PubMed, 208 citations in OpenAlex.
- Starch phosphorylase acts as a pivotal scaffold connecting starch metabolism enzymes with photosystem I subunits.Plant & cell physiology · 2026Article
- HvPHO1 Controls a Glucose 1-Phosphate-SnRK1 Signalling Module That Coordinates Starch Accumulation in Barley Endosperm.Plant biotechnology journal · 2026Article
- Subclass III SnRK2 Kinases Coordinate Starch and Storage Protein Synthesis During Maize Kernel Development.Plant biotechnology journal · 2026Article
- Moderate Regulation of SBEIIb Gene Expression by Editing Cis-Regulatory Elements Enhances the Resistant Starch Content in Rice.Plant biotechnology journal · 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
- Simultaneous Repression of GLUCAN WATER DIKINASE 1 and STARCH BRANCHING ENZYME 1 in Potato Tubers Leads to Starch With Increased Amylose and Novel Industrial Properties.Biotechnology journal · 2025Article
- Stimulus-responsive proteins involved in multi-process regulation of storage substance accumulation during rice grain filling under elevated temperature.BMC plant biology · 2023Article
- Soluble and insoluble α-glucan synthesis in yeast by enzyme suites derived exclusively from maize endosperm.Plant physiology · 2023Article
- Gene expression profile of the developing endosperm in durum wheat provides insight into starch biosynthesis.BMC plant biology · 2023Article
- Genetic Engineering of Starch Biosynthesis in Maize Seeds for Efficient Enzymatic Digestion of Starch during Bioethanol Production.International journal of molecular sciences · 2023Review
- 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
- The Function of DNA Demethylase Gene ROS1a Null Mutant on Seed Development in Rice (International journal of molecular sciences · 2022Article
- Resistant starch formation in rice: Genetic regulation and beyond.Plant communications · 2022Review
- Analysis of Global Gene Expression in Maize (Plants (Basel, Switzerland) · 2022Article
- Profiling of transcriptional regulators associated with starch biosynthesis in sorghum (Frontiers in plant science · 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
28 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Starch biosynthetic enzymes from maize (Zea mays) and wheat (Triticum aestivum) amyloplasts exist in cell extracts in high molecular weight complexes; however, the nature of those assemblies remains to be defined. This study tested the interdependence of the maize enzymes starch synthase IIa (SSIIa), SSIII, starch branching enzyme IIb (SBEIIb), and SBEIIa for assembly into multisubunit complexes. Mutations that eliminated any one of those proteins also prevented the others from assembling into a high molecular mass form of approximately 670 kD, so that SSIII, SSIIa, SBEIIa, and SBEIIb most likely all exist together in the same complex. SSIIa, SBEIIb, and SBEIIa, but not SSIII, were also interdependent for assembly into a complex of approximately 300 kD. SSIII, SSIIa, SBEIIa, and SBEIIb copurified through successive chromatography steps, and SBEIIa, SBEIIb, and SSIIa coimmunoprecipitated with SSIII in a phosphorylation-dependent manner. SBEIIa and SBEIIb also were retained on an affinity column bearing a specific conserved fragment of SSIII located outside of the SS catalytic domain. Additional proteins that copurified with SSIII in multiple biochemical methods included the two known isoforms of pyruvate orthophosphate dikinase (PPDK), large and small subunits of ADP-glucose pyrophosphorylase, and the sucrose synthase isoform SUS-SH1. PPDK and SUS-SH1 required SSIII, SSIIa, SBEIIa, and SBEIIb for assembly into the 670-kD complex. These complexes may function in global regulation of carbon partitioning between metabolic pathways in developing seeds.
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