LIKE EARLY STARVATION 1 and EARLY STARVATION 1 promote and stabilize amylopectin phase transition in starch biosynthesis
Autor: | Chun Liu, Barbara Pfister, Rayan Osman, Maximilian Ritter, Arvid Heutinck, Mayank Sharma, Simona Eicke, Michaela Fischer-Stettler, David Seung, Coralie Bompard, Melanie R. Abt, Samuel C. Zeeman |
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Přispěvatelé: | Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] (ETH Zürich), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF) |
Jazyk: | angličtina |
Rok vydání: | 2023 |
Předmět: | |
Zdroj: | Science Advances Science Advances, 2023, Science Advances, 9 (21), pp.eadg7448. ⟨10.1126/sciadv.adg7448⟩ Science Advances, 9 (21) |
ISSN: | 2375-2548 |
DOI: | 10.1126/sciadv.adg7448⟩ |
Popis: | Starch, the most abundant carbohydrate reserve in plants, primarily consists of the branched glucan amylopectin, which forms semi-crystalline granules. Phase transition from a soluble to an insoluble form depends on amylopectin architecture, requiring a compatible distribution of glucan chain lengths and a branch-point distribution. Here, we show that two starch-bound proteins, LIKE EARLY STARVATION 1 (LESV) and EARLY STARVATION 1 (ESV1), which have unusual carbohydrate-binding surfaces, promote the phase transition of amylopectin-like glucans, both in a heterologous yeast system expressing the starch biosynthetic machinery and in Arabidopsis plants. We propose a model wherein LESV serves as a nucleating role, with its carbohydrate-binding surfaces helping align glucan double helices to promote their phase transition into semi-crystalline lamellae, which are then stabilized by ESV1. Because both proteins are widely conserved, we suggest that protein-facilitated glucan crystallization may be a general and previously unrecognized feature of starch biosynthesis. Science Advances, 9 (21) ISSN:2375-2548 |
Databáze: | OpenAIRE |
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