title: Structure-based view on [PSI(+)] prion properties.
abstract: Yeast [PSI(+)] prion is one of the most suitable and well characterized system for the investigation of the prion phenomenon. However, until recently, the lack of data on the 3D arrangement of Sup35p prion fibrils hindered progress in this area. The recent arrival in this field of new experimental techniques led to the parallel and in-register superpleated β-structure as a consensus model for Sup35p fibrils. Here, we analyzed the effect of amino acid substitutions of the Sup35 protein through the prism of this structural model. Application of a newly developed computational approach, called ArchCandy, gives us a better understanding of the effect caused by mutations on the fibril forming potential of Sup35 protein. This bioinformatics tool can be used for the design of new mutations with desired modification of prion properties. Thus, we provide examples of how today, having progress toward elucidation of the structural arrangement of Sup35p fibrils, researchers can advance more efficiently to a better understanding of prion [PSI(+)] stability and propagation.
authors.affiliation: a Department of Genetics and Biotechnology ; St. Petersburg State University ; St. Petersburg , Russia.
authors.forename: Stanislav A
authors.initials: SA
authors.lastname: Bondarev
authors.forename: Galina A
authors.initials: GA
authors.lastname: Zhouravleva
authors.forename: Mikhail V
authors.initials: MV
authors.lastname: Belousov
authors.forename: Andrey V
authors.initials: AV
authors.lastname: Kajava
mesh_terms: D000595:Amino Acid Sequence; D019295:Computational Biology; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D011328:Prions / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D012984:Software
chemical_list: D011328:Prions
keywords: Asu mutations, antisupressor mutations; EM, electron microscopy; NMR, nuclear magnetic resonance; PNM, [PSI+] no more; STEM, scanning transmission electron microscopy; amyloid, prion, protein misfolding, protein structure, Saccharomyces cerevisiae, superpleated β-structure, [PSI+]