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

Autor: Antonets KS; All-Russia Research Institute for Agricultural Microbiology (ARRIAM), St. Petersburg, Russia.; St. Petersburg State University, St. Petersburg, Russia., Belousov MV; All-Russia Research Institute for Agricultural Microbiology (ARRIAM), St. Petersburg, Russia.; St. Petersburg State University, St. Petersburg, Russia., Sulatskaya AI; Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia., Belousova ME; All-Russia Research Institute for Agricultural Microbiology (ARRIAM), St. Petersburg, Russia., Kosolapova AO; All-Russia Research Institute for Agricultural Microbiology (ARRIAM), St. Petersburg, Russia.; St. Petersburg State University, St. Petersburg, Russia., Sulatsky MI; Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia., Andreeva EA; St. Petersburg State University, St. Petersburg, Russia., Zykin PA; St. Petersburg State University, St. Petersburg, Russia., Malovichko YV; All-Russia Research Institute for Agricultural Microbiology (ARRIAM), St. Petersburg, Russia.; St. Petersburg State University, St. Petersburg, Russia., Shtark OY; All-Russia Research Institute for Agricultural Microbiology (ARRIAM), St. Petersburg, Russia., Lykholay AN; St. Petersburg State University, St. Petersburg, Russia., Volkov KV; St. Petersburg State University, St. Petersburg, Russia., Kuznetsova IM; Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia., Turoverov KK; Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia., Kochetkova EY; Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia., Bobylev AG; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, Russia., Usachev KS; Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, Kazan, Russia., Demidov ON; Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia.; INSERM UMR1231, UBFC, Dijon, France., Tikhonovich IA; All-Russia Research Institute for Agricultural Microbiology (ARRIAM), St. Petersburg, Russia.; St. Petersburg State University, St. Petersburg, Russia., Nizhnikov AA; All-Russia Research Institute for Agricultural Microbiology (ARRIAM), St. Petersburg, Russia.; St. Petersburg State University, St. Petersburg, Russia.
Jazyk: angličtina
Zdroj: PLoS biology [PLoS Biol] 2020 Jul 23; Vol. 18 (7), pp. e3000564. Date of Electronic Publication: 2020 Jul 23 (Print Publication: 2020).
DOI: 10.1371/journal.pbio.3000564
Abstrakt: 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.
Competing Interests: The authors have declared that no competing interests exist.
Databáze: MEDLINE
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