ArticleThe Journal of biological chemistry2016
Rice Endosperm Starch Phosphorylase (Pho1) Assembles with Disproportionating Enzyme (Dpe1) to Form a Protein Complex That Enhances Synthesis of Malto-oligosaccharides.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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39 citing papers in PubMed, 94 citations in OpenAlex.
- Starch phosphorylase acts as a pivotal scaffold connecting starch metabolism enzymes with photosystem I subunits.Plant & cell physiology · 2026Article
- Regulatory factors of starch metabolism in cereal endosperm.Plant molecular biology · 2026Review
- The plastidial PHS1-DPE1 complex drives efficient malto-oligosaccharides synthesis in rice starch metabolism.Nature communications · 2026Article
- A structural perspective on α-glucan catabolism in oxygenic phototrophs.The Plant journal : for cell and molecular biology · 2026Review
- Genome-wide association studies for identification of QTLs and key candidate genes to improve grain quality in rice (Food chemistry. Molecular sciences · 2025Article
- Old player, new roles: defining the role of the plastidial phosphorylase.The New phytologist · 2025Review
- Functional Modification and Applications of Rice Starch Emulsion Systems Based on Interfacial Engineering.Foods (Basel, Switzerland) · 2025Review
- Plastidial starch phosphorylase regulates maltodextrin turnover during starch granule initiation in Arabidopsis leaves.Plant physiology · 2025Article
- Kinetic and Structural Studies of the PlastidialACS omega · 2024Article
- Spatiotemporal transcriptomic atlas of rhizome formation in Oryza longistaminata.Plant biotechnology journal · 2024Article
- Dynamics of starch formation and gene expression during grain filling and its possible influence on grain quality.Scientific reports · 2024Article
- Transcriptomics and starch biosynthesis analysis in leaves and developing seeds of mung bean provide a basis for genetic engineering of starch composition and seed quality.Frontiers in plant science · 2024Article
- Initiation of B-type starch granules in wheat endosperm requires the plastidial α-glucan phosphorylase PHS1.The Plant cell · 2023Article
- Site-Directed Mutations at Phosphorylation Sites inPlants (Basel, Switzerland) · 2023Article
- Article
- Gene expression profile of the developing endosperm in durum wheat provides insight into starch biosynthesis.BMC plant biology · 2023Article
- The Plastidial Glucan Phosphorylase Affects the Maltooligosaccharide Metabolism in Parenchyma Cells of Potato (Solanum tuberosum L.) Tuber Discs.Plant & cell physiology · 2023Article
- Pho1 cooperates with DPE1 to control short maltooligosaccharide mobilization during starch synthesis initiation in rice endosperm.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2023Article
- Low-temperature at booting reduces starch content and yield of wheat by affecting dry matter transportation and starch synthesis.Frontiers in plant science · 2023Article
- Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Starch synthesis in cereal grain endosperm is dependent on the concerted actions of many enzymes. The starch plastidial phosphorylase (Pho1) plays an important role in the initiation of starch synthesis and in the maturation of starch granule in developing rice seeds. Prior evidence has suggested that the rice enzyme, OsPho1, may have a physical/functional interaction with other starch biosynthetic enzymes. Pulldown experiments showed that OsPho1 as well as OsPho1 devoid of its L80 region, a peptide unique to higher plant phosphorylases, captures disproportionating enzyme (OsDpe1). Interaction of the latter enzyme form with OsDpe1 indicates that the putative regulatory L80 is not responsible for multienzyme assembly. This heterotypic enzyme complex, determined at a molar ratio of 1:1, was validated by reciprocal co-immunoprecipitation studies of native seed proteins and by co-elution chromatographic and co-migration electrophoretic patterns of these enzymes in rice seed extracts. The OsPho1-OsDpe1 complex utilized a broader range of substrates for enhanced synthesis of larger maltooligosaccharides than each individual enzyme and significantly elevated the substrate affinities of OsPho1 at 30 °C. Moreover, the assembly with OsDpe1 enables OsPho1 to utilize products of transglycosylation reactions involving G1 and G3, sugars that it cannot catalyze directly.
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