title: Amyloid of the Candida albicans Ure2p prion domain is infectious and has an in-register parallel β-sheet structure.
abstract: Ure2p of Candida albicans (Ure2(albicans) or CaUre2p) can be a prion in Saccharomyces cerevisiae, but Ure2p of Candida glabrata (Ure2(glabrata)) cannot, even though the Ure2(glabrata) N-terminal domain is more similar to that of the S. cerevisiae Ure2p (Ure2(cerevisiae)) than Ure2(albicans) is. We show that the N-terminal N/Q-rich prion domain of Ure2(albicans) forms amyloid that is infectious, transmitting [URE3alb] to S. cerevisiae cells expressing only C. albicans Ure2p. Using solid-state nuclear magnetic resonance of selectively labeled C. albicans Ure2p(1-90), we show that this infectious amyloid has an in-register parallel β-sheet structure, like that of the S. cerevisiae Ure2p prion domain and other S. cerevisiae prion amyloids. In contrast, the N/Q-rich N-terminal domain of Ure2(glabrata) does not readily form amyloid, and that formed upon prolonged incubation is not infectious.
authors.affiliation: Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0830, USA.
authors.forename: Abbi
authors.initials: A
authors.lastname: Engel
authors.forename: Frank
authors.initials: F
authors.lastname: Shewmaker
authors.forename: Herman K
authors.initials: HK
authors.lastname: Edskes
authors.forename: Fred
authors.initials: F
authors.lastname: Dyda
authors.forename: Reed B
authors.initials: RB
authors.lastname: Wickner
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000502:physiology; D002176:Candida albicans / Q000737:chemistry* / Q000472:pathogenicity; D041221:Candida glabrata / Q000737:chemistry; D015964:Gene Expression Regulation, Bacterial; D005979:Glutathione Peroxidase / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D017096:Prion Diseases / Q000382:microbiology*; D011328:Prions / Q000096:biosynthesis* / Q000737:chemistry* / Q000472:pathogenicity* / Q000502:physiology; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000472:pathogenicity; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry
chemical_list: D000682:Amyloid; D011328:Prions; D029701:Saccharomyces cerevisiae Proteins; D005979:Glutathione Peroxidase; C067020:URE2 protein, S cerevisiae