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Accumulation of storage proteins in plant seeds is mediated by amyloid formation

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dc.contributor.author Antonets K.S.
dc.contributor.author Belousov M.V.
dc.contributor.author Sulatskaya A.I.
dc.contributor.author Belousova M.E.
dc.contributor.author Kosolapova A.O.
dc.contributor.author Sulatsky M.I.
dc.contributor.author Andreeva E.A.
dc.contributor.author Zykin P.A.
dc.contributor.author Malovichko Y.V.
dc.contributor.author Shtark O.Y.
dc.contributor.author Lykholay A.N.
dc.contributor.author Volkov K.V.
dc.contributor.author Kuznetsova I.M.
dc.contributor.author Turoverov K.K.
dc.contributor.author Kochetkova E.Y.
dc.contributor.author Bobylev A.G.
dc.contributor.author Usachev K.S.
dc.contributor.author Demidov O.N.
dc.contributor.author Tikhonovich I.A.
dc.contributor.author Nizhnikov A.A.
dc.date.accessioned 2021-02-25T20:43:47Z
dc.date.available 2021-02-25T20:43:47Z
dc.date.issued 2020
dc.identifier.issn 1544-9173
dc.identifier.uri https://dspace.kpfu.ru/xmlui/handle/net/162324
dc.description.abstract Copyright: © 2020 Antonets et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Amyloids are protein aggregates with a highly ordered spatial structure giving them unique physicochemical properties. Different amyloids not only participate in the development of numerous incurable diseases but control vital functions in archaea, bacteria and eukarya. Plants are a poorly studied systematic group in the field of amyloid biology. Amyloid properties have not yet been demonstrated for plant proteins under native conditions in vivo. Here we show that seeds of garden pea Pisum sativum L. contain amyloid-like aggregates of storage proteins, the most abundant one, 7S globulin Vicilin, forms bona fide amyloids in vivo and in vitro. Full-length Vicilin contains 2 evolutionary conserved β-barrel domains, Cupin-1.1 and Cupin-1.2, that self-assemble in vitro into amyloid fibrils with similar physicochemical properties. However, Cupin-1.2 fibrils unlike Cupin-1.1 can seed Vicilin fibrillation. In vivo, Vicilin forms amyloids in the cotyledon cells that bind amyloid-specific dyes and possess resistance to detergents and proteases. The Vicilin amyloid accumulation increases during seed maturation and wanes at germination. Amyloids of Vicilin resist digestion by gastrointestinal enzymes, persist in canned peas, and exhibit toxicity for yeast and mammalian cells. Our finding for the first time reveals involvement of amyloid formation in the accumulation of storage proteins in plant seeds.
dc.relation.ispartofseries PLoS Biology
dc.title Accumulation of storage proteins in plant seeds is mediated by amyloid formation
dc.type Article
dc.relation.ispartofseries-issue 7
dc.relation.ispartofseries-volume 18
dc.collection Публикации сотрудников КФУ
dc.source.id SCOPUS15449173-2020-18-7-SID85088510561


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  • Публикации сотрудников КФУ Scopus [24551]
    Коллекция содержит публикации сотрудников Казанского федерального (до 2010 года Казанского государственного) университета, проиндексированные в БД Scopus, начиная с 1970г.

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