Amyloidogenic domains, prions and structural inheritance: rudiments of early life or recent acquisition?
Amyloids are self-assembled fibre-like beta-rich protein aggregates. Amyloidogenic prion proteins propagate amyloid state in vivo and transmit it via infection or in cell divisions. While amyloid aggregation may occur in the absence of any other proteins, in vivo propagation of the amyloid state requires chaperone helpers. Yeast prion proteins contain prion domains which include distinct aggregation and propagation elements, responsible for these functions. Known aggregation and propagation elements are short in length and composed of relatively simple sequences, indicating possible ancient origin. Prion-like self-assembled structures could be involved in the initial steps of biological compartmentalization in early life.
Chernoff
Yury O
YO
School of Biology and Institute for Bioengineering and Bioscience, Georgia Institute of Technology, 315 Ferst Drive, Atlanta, Georgia 30332-0363, USA. yury.chernoff@biology.gatech.edu
D000682:Amyloid / Q000096:biosynthesis*; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D008954:Models, Biological; D018832:Molecular Chaperones / Q000378:metabolism; D011328:Prions / Q000235:genetics / Q000378:metabolism*; D015003:Yeasts / Q000235:genetics / Q000378:metabolism
D000682:Amyloid; D005656:Fungal Proteins; D018832:Molecular Chaperones; D011328:Prions