Accumulation of storage proteins in plant seeds is mediated by amyloid formation.
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 s...
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Format: | Article |
Language: | English |
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Public Library of Science (PLoS)
2020-07-01
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Series: | PLoS Biology |
Online Access: | https://doi.org/10.1371/journal.pbio.3000564 |
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author | Kirill S Antonets Mikhail V Belousov Anna I Sulatskaya Maria E Belousova Anastasiia O Kosolapova Maksim I Sulatsky Elena A Andreeva Pavel A Zykin Yury V Malovichko Oksana Y Shtark Anna N Lykholay Kirill V Volkov Irina M Kuznetsova Konstantin K Turoverov Elena Y Kochetkova Alexander G Bobylev Konstantin S Usachev Oleg N Demidov Igor A Tikhonovich Anton A Nizhnikov |
author_facet | Kirill S Antonets Mikhail V Belousov Anna I Sulatskaya Maria E Belousova Anastasiia O Kosolapova Maksim I Sulatsky Elena A Andreeva Pavel A Zykin Yury V Malovichko Oksana Y Shtark Anna N Lykholay Kirill V Volkov Irina M Kuznetsova Konstantin K Turoverov Elena Y Kochetkova Alexander G Bobylev Konstantin S Usachev Oleg N Demidov Igor A Tikhonovich Anton A Nizhnikov |
author_sort | Kirill S Antonets |
collection | DOAJ |
description | 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. |
first_indexed | 2024-12-18T02:11:30Z |
format | Article |
id | doaj.art-f8927a4807e746d39343a88533d84ce8 |
institution | Directory Open Access Journal |
issn | 1544-9173 1545-7885 |
language | English |
last_indexed | 2024-12-18T02:11:30Z |
publishDate | 2020-07-01 |
publisher | Public Library of Science (PLoS) |
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spelling | doaj.art-f8927a4807e746d39343a88533d84ce82022-12-21T21:24:29ZengPublic Library of Science (PLoS)PLoS Biology1544-91731545-78852020-07-01187e300056410.1371/journal.pbio.3000564Accumulation of storage proteins in plant seeds is mediated by amyloid formation.Kirill S AntonetsMikhail V BelousovAnna I SulatskayaMaria E BelousovaAnastasiia O KosolapovaMaksim I SulatskyElena A AndreevaPavel A ZykinYury V MalovichkoOksana Y ShtarkAnna N LykholayKirill V VolkovIrina M KuznetsovaKonstantin K TuroverovElena Y KochetkovaAlexander G BobylevKonstantin S UsachevOleg N DemidovIgor A TikhonovichAnton A NizhnikovAmyloids 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.https://doi.org/10.1371/journal.pbio.3000564 |
spellingShingle | Kirill S Antonets Mikhail V Belousov Anna I Sulatskaya Maria E Belousova Anastasiia O Kosolapova Maksim I Sulatsky Elena A Andreeva Pavel A Zykin Yury V Malovichko Oksana Y Shtark Anna N Lykholay Kirill V Volkov Irina M Kuznetsova Konstantin K Turoverov Elena Y Kochetkova Alexander G Bobylev Konstantin S Usachev Oleg N Demidov Igor A Tikhonovich Anton A Nizhnikov Accumulation of storage proteins in plant seeds is mediated by amyloid formation. PLoS Biology |
title | Accumulation of storage proteins in plant seeds is mediated by amyloid formation. |
title_full | Accumulation of storage proteins in plant seeds is mediated by amyloid formation. |
title_fullStr | Accumulation of storage proteins in plant seeds is mediated by amyloid formation. |
title_full_unstemmed | Accumulation of storage proteins in plant seeds is mediated by amyloid formation. |
title_short | Accumulation of storage proteins in plant seeds is mediated by amyloid formation. |
title_sort | accumulation of storage proteins in plant seeds is mediated by amyloid formation |
url | https://doi.org/10.1371/journal.pbio.3000564 |
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