Amyloids and prions in the light of evolution.

Autor: Galkin AP; Vavilov Institute of General Genetics, St. Petersburg Branch, Russian Academy of Sciences, St. Petersburg, Russian Federation, 199034. apgalkin@mail.ru.; Department of Genetics and Biotechnology, St. Petersburg State University, St. Petersburg, Russian Federation, 199034. apgalkin@mail.ru., Sysoev EI; Vavilov Institute of General Genetics, St. Petersburg Branch, Russian Academy of Sciences, St. Petersburg, Russian Federation, 199034.; Department of Genetics and Biotechnology, St. Petersburg State University, St. Petersburg, Russian Federation, 199034., Valina AA; Department of Genetics and Biotechnology, St. Petersburg State University, St. Petersburg, Russian Federation, 199034.
Jazyk: angličtina
Zdroj: Current genetics [Curr Genet] 2023 Dec; Vol. 69 (4-6), pp. 189-202. Date of Electronic Publication: 2023 May 10.
DOI: 10.1007/s00294-023-01270-6
Abstrakt: Functional amyloids have been identified in a wide variety of organisms including bacteria, fungi, plants, and vertebrates. Intracellular and extracellular amyloid fibrils of different proteins perform storage, protective, structural, and regulatory functions. The structural organization of amyloid fibrils determines their unique physical and biochemical properties. The formation of these fibrillar structures can provide adaptive advantages that are picked up by natural selection. Despite the great interest in functional and pathological amyloids, questions about the conservatism of the amyloid properties of proteins and the regularities in the appearance of these fibrillar structures in evolution remain almost unexplored. Using bioinformatics approaches and summarizing the data published previously, we have shown that amyloid fibrils performing similar functions in different organisms have been arising repeatedly and independently in the course of evolution. On the other hand, we show that the amyloid properties of a number of bacterial and eukaryotic proteins are evolutionarily conserved. We also discuss the role of protein-based inheritance in the evolution of microorganisms. Considering that missense mutations and the emergence of prions cause the same consequences, we propose the concept that the formation of prions, similarly to mutations, generally causes a negative effect, although it can also lead to adaptations in rare cases. In general, our analysis revealed certain patterns in the emergence and spread of amyloid fibrillar structures in the course of evolution.
(© 2023. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.)
Databáze: MEDLINE
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