Functional amyloids of eukaryotes: criteria, classification, and biological significance
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REVIEW
Functional amyloids of eukaryotes: criteria, classification, and biological significance Aleksandra V. Sergeeva2 · Alexey P. Galkin1,2 Received: 26 March 2020 / Revised: 16 April 2020 / Accepted: 20 April 2020 © Springer-Verlag GmbH Germany, part of Springer Nature 2020
Abstract Amyloids cause incurable diseases in humans and animals and regulate vital processes in bacteria and eukaryotes. Amyloid fibrils have unique properties, such as amazing resistance to a variety of agents, mechanical strength, and elasticity, and it is not surprising that in the course of evolution eukaryotes have learned to employ amyloid structures to regulate various vital processes. Proteins exhibiting amyloid properties have been detected in lower eukaryotes and in diverse cell lines of arthropods and vertebrates. A growing number of studies of eukaryotic proteins that demonstrate certain amyloid-like properties require clear criteria to systematize modern knowledge about the functional amyloids. In this review, we propose to separate eukaryotic proteins, whose amyloid properties are clearly proven, and proteins, which show some amyloid characteristics in vivo or in vitro. In order to assert that a protein is a functional amyloid, it is necessary to prove that it has a cross-β structure in vivo. Here, we consider the advantages and disadvantages of various methods for the analysis of the amyloid properties of a protein. Analysis of the current data shows that amyloids play an important role in the regulation of vital processes in eukaryotes, and new functional amyloids should be searched primarily among structural, protective, and storage proteins. A systematic search for functional amyloids in eukaryotes is only beginning, and the use of novel proteomic methods opens up great prospects for identification of amyloids in any organs and tissues of various organisms. Keywords Functional amyloids · Amyloid-like proteins · Eukaryotes · Criteria · Classification
Introduction. Criteria for the identification of functional amyloids of eukaryotes Amyloids are fibrillar proteins possessing a cross-β conformation in vivo. The cross-β structure is formed by β-sheets running parallel to each other and perpendicular to the long axis of the fibrils (Sunde and Blake 1997). The term amyloid was traditionally used to describe extracellular pathological tissue deposits of protein fibrils, recognized by specific properties, such as yellow-green birefringence after staining with Congo red (CR) (Benson et al. 2018). However, to date, Communicated by M. Kupiec. * Alexey P. Galkin [email protected] 1
Vavilov Institute of General Genetics, St. Petersburg Branch, Russian Academy of Sciences, 199034 St. Petersburg, Russian Federation
Department of Genetics and Biotechnology, St. Petersburg State University, 199034 St. Petersburg, Russian Federation
2
a number of bacterial and eukaryotic proteins have been identified that form intracellular and extracellular fibrils with cross-β structure, that regulate vital processes. Such proteins are comm
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