[Yeast prions, mammalian amyloidoses, and the problem of proteomic networks].
Prion proteins are infective amyloids and cause several neurodegenerative diseases in humans and animals. In yeasts, prions are expressed as cytoplasmic heritable determinants of a protein nature. Yeast prion [PSI], which results from a conformational rearrangement and oligomerization of translation termination factor eRF3, is used as an example to consider the structural--functional relationships in a potentially prion molecule, specifics of its evolution, and interactions with other prions, which form so-called prion networks. In addition, the review considers the results of modeling mammalian prion diseases and other amyloidoses in yeast cells. A hypothesis of proteomic networks is proposed by analogy with prion networks, involving interactions of different amyloids in mammals.
Galkin
A P
AP
Mironova
L N
LN
Zhuravleva
G A
GA
Inge-Vechtomov
S G
SG
D000682:Amyloid / Q000737:chemistry / Q000378:metabolism; D000686:Amyloidosis / Q000378:metabolism*; D006801:Humans; D008954:Models, Biological; D010454:Peptide Termination Factors; D017096:Prion Diseases / Q000378:metabolism*; D011328:Prions / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D020543:Proteome / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*
D000682:Amyloid; D010454:Peptide Termination Factors; D011328:Prions; D020543:Proteome; C068068:SUP35 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins