Yeast Prions Compared to Functional Prions and Amyloids.
Yeast Prions Compared to Functional Prions and Amyloids.
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DOI:
10.1016/j.jmb.2018.04.022
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发表时间:
2018-10
影响因子:
5.6
通讯作者:
R. Wickner;H. Edskes;Moonil Son;E. Bezsonov;Morgan DeWilde;Mathieu Ducatez
中科院分区:
文献类型:
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作者:
R. Wickner;H. Edskes;Moonil Son;E. Bezsonov;Morgan DeWilde;Mathieu Ducatez
Saccharomyces cerevisiae is an occasional host to an array of prions, most based on self-propagating, self-templating amyloid filaments of a normally soluble protein. [URE3] is a prion of Ure2p, a regulator of nitrogen catabolism, while [PSI +] is a prion of Sup35p, a subunit of the translation termination factor Sup35p. In contrast to the functional prions, [Het-s] of Podospora anserina and [BETA] of yeast, the amyloid-based yeast prions are rare in wild strains, arise sporadically, have an array of prion variants for a single prion protein sequence, have a folded in-register parallel β-sheet amyloid architecture, are detrimental to their hosts, arouse a stress response in the host, and are subject to curing by various host anti-prion systems. These characteristics allow a logical basis for distinction between functional amyloids/prions and prion diseases. These infectious yeast amyloidoses are outstanding models for the many common human amyloid-based diseases that are increasingly found to have some infectious characteristics.