LIKE EARLY STARVATION 1 and EARLY STARVATION ...
Type de document :
Article dans une revue scientifique: Article original
DOI :
URL permanente :
Titre :
LIKE EARLY STARVATION 1 and EARLY STARVATION 1 promote and stabilize amylopectin phase transition in starch biosynthesis
Auteur(s) :
Liu, Chun [Auteur]
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] [ETH Zürich]
Pfister, Barbara [Auteur]
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] [ETH Zürich]
Osman, Rayan [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Ritter, Maximilian [Auteur]
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] [ETH Zürich]
Heutinck, Arvid [Auteur]
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] [ETH Zürich]
Sharma, Mayank [Auteur]
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] [ETH Zürich]
Eicke, Simona [Auteur]
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] [ETH Zürich]
Fischer-Stettler, Michaela [Auteur]
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] [ETH Zürich]
Seung, David [Auteur]
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] [ETH Zürich]
Bompard, Coralie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Abt, Melanie R. [Auteur]
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] [ETH Zürich]
Zeeman, Samuel C. [Auteur]
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] [ETH Zürich]
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] [ETH Zürich]
Pfister, Barbara [Auteur]
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] [ETH Zürich]
Osman, Rayan [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Ritter, Maximilian [Auteur]
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] [ETH Zürich]
Heutinck, Arvid [Auteur]
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] [ETH Zürich]
Sharma, Mayank [Auteur]
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] [ETH Zürich]
Eicke, Simona [Auteur]
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] [ETH Zürich]
Fischer-Stettler, Michaela [Auteur]
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] [ETH Zürich]
Seung, David [Auteur]
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] [ETH Zürich]
Bompard, Coralie [Auteur]
![refId](/themes/Mirage2//images/idref.png)
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Abt, Melanie R. [Auteur]
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] [ETH Zürich]
Zeeman, Samuel C. [Auteur]
Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] [ETH Zürich]
Titre de la revue :
Science Advances
Nom court de la revue :
Sci. Adv.
Numéro :
9
Pagination :
eadg7448
Éditeur :
American Association for the Advancement of Science (AAAS)
Date de publication :
2023-05-26
ISSN :
2375-2548
Discipline(s) HAL :
Sciences du Vivant [q-bio]
Chimie/Chimie théorique et/ou physique
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
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 ...
Lire la suite >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.Lire moins >
Lire la suite >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.Lire moins >
Langue :
Anglais
Audience :
Internationale
Vulgarisation :
Non
Établissement(s) :
Université de Lille
CNRS
CNRS
Équipe(s) de recherche :
Plant Storage Polysaccharides
Date de dépôt :
2023-07-12T14:09:52Z
2023-07-13T09:12:48Z
2023-07-13T09:12:48Z
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- P23.12 sciadv.adg7448.pdf
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