Abstract：
: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.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Wickner RB,Edskes HK,Son M,Bezsonov EE,DeWilde M,Ducatez Mdoi
10.1016/j.jmb.2018.04.022subject
Has Abstractpub_date
2018-10-12 00:00:00pages
3707-3719issue
20eissn
0022-2836issn
1089-8638pii
S0022-2836(18)30275-4journal_volume
430pub_type
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