Yeast Prions Compared to Functional Prions and Amyloids. Issue 20 (12th October 2018)

• Record Type: Journal Article
• Authors: Wickner, Reed B.; Edskes, Herman K.; Son, Moonil; Bezsonov, Evgeny E.; DeWilde, Morgan; Ducatez, Mathieu
• Is Part Of: Journal of molecular biology. Volume 430:Issue 20(2018)
• Page Start: 3707
• Page End: 3719
• Publication Date: 2018-10-12
• Subjects: anti-prion systems -- amyloid of Sup35 or Ure2 -- inositol polyphosphates -- Upf, Btn2p, Cur1p, Hsp104, Ssb1, Siw14 -- folded in-register parallel beta sheets; Molecular biology -- Periodicals; Biology -- Periodicals; Biochemistry -- Periodicals; Bacteriology -- Periodicals; Molecular Biology -- Periodicals; Biochemistry -- Periodicals; Biologie moléculaire -- Périodiques; Biologie -- Périodiques; Biochimie -- Périodiques; Moleculaire biologie; Biochemistry; Biology; Molecular biology; Periodicals; 572.805
• DOI: 10.1016/j.jmb.2018.04.022
• Languages: English
• ISSNs: 0022-2836

Abstract

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. Graphical abstract: Highlights: Pathogenic prions (like yeast prions) are rare in wild strains, but functional prions/amyloids are common in the wild. Pathogenic prions come in many variants, each self-propagating and based on a single protein. Functional prion/amyloids have a single (optimized) structure/variant. Pathogenic prions/amyloids are usually folded in-register parallel beta sheets. The functional prion [Het-s] has a beta-helix amyloid structure. Pathologic prions are subject to an array of anti-prion systems, while functional prions/amyloids are not.