[Structure and functional similarity of yeast Sup35p and Ure2p proteins to mammalian prions].
The results of studies of yeast cytoplasmically-inherited determinants [psi] and [URE3] are summarized. The existence of tandem amino acid repeats in N-terminal regions of yeast Sup35p protein and in prions of higher eukaryotes is shown. The prion-like properties of yeast Sup35p and Ure2p proteins and a role of tandem amino acid repeats localized in N-terminal region of Sup35p protein in inheritance of [psi] determinants is discussed. The suggestion is made that the [psi+] status of yeast cell depends on the specific conformation of the N-terminal domain of Sup35p and that this protein can induce the specific conformational state of its N-terminal domain on newly synthesized Sup35p molecules via protein-protein interaction, thus representing a molecular basis of inheritance of [psi+] determinant. Other proteins containing amino acid repeats of similar type are considered and the suggestion is made that some of these proteins may show prion-like behavior.
D000595:Amino Acid Sequence; D000818:Animals; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D008322:Mammals; D008969:Molecular Sequence Data; D011328:Prions / Q000737:chemistry*; D011485:Protein Binding; D012441:Saccharomyces cerevisiae / Q000737:chemistry*; D013329:Structure-Activity Relationship
D005656:Fungal Proteins; D011328:Prions
Strukturnoe i funktsional'noe skhodstvo belkov Sup35p i Ure2p drozhzheĭ s prionami mlekopitaiushchikh.