title: Fungal prions: structure, function and propagation.
abstract: Prions are not uniquely associated with rare fatal neurodegenerative diseases in the animal kingdom; prions are also found in fungi and in particular the yeast Saccharomyces cerevisiae. As with animal prions, fungal prions are proteins able to exist in one or more self-propagating alternative conformations, but show little primary sequence relationship with the mammalian prion protein PrP. Rather, fungal prions represent a relatively diverse collection of proteins that participate in key cellular processes such as transcription and translation. Upon switching to their prion form, these proteins can generate stable, sometimes beneficial, changes in the host cell phenotype. Much has already been learnt about prion structure, and propagation and de novo generation of the prion state through studies in yeast and these findings are reviewed here.
authors: Kent Fungal Group, School of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, UK. M.F.Tuite@kent.ac.uk
authors: Mick F
authors: MF
authors: Tuite
authors: Ricardo
authors: R
authors: Marchante
authors: Vitaly
authors: V
authors: Kushnirov
mesh_terms: D000682:Amyloid / Q000737:chemistry; D005656:Fungal Proteins / Q000737:chemistry*; D015966:Gene Expression Regulation, Fungal; D014644:Genetic Variation; D018832:Molecular Chaperones / Q000378:metabolism; D048468:Podospora / Q000378:metabolism; D011328:Prions / Q000737:chemistry*; D014176:Protein Biosynthesis; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry; D014158:Transcription, Genetic
chemical_list: D000682:Amyloid; D005656:Fungal Proteins; D018832:Molecular Chaperones; D011328:Prions; D029701:Saccharomyces cerevisiae Proteins