Primary sequence independence for prion formation

Many proteins can adopt self-propagating beta-sheet-rich structures, termed amyloid fibrils. The URE3 and PSI(+) prions of Saccharomyces cerevisiae are infectious amyloid forms of the proteins Ure2p and Sup35p, respectively. Ure2p forms prions primarily as a result of its sequence composition, as ve...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2005-09, Vol.102 (36), p.12825-12830
Hauptverfasser:	Ross, E.D, Edskes, H.K, Terry, M.J, Wickner, R.B
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence amino acid sequences Amino acids Amyloid - chemistry Amyloid - metabolism amyloid protein Amyloids Biological Sciences Cell growth fungal proteins Genetics Glutathione Peroxidase Molecular Sequence Data Oligonucleotides Peptide Termination Factors Phenotype Phenotypes Plasmids Polymerase chain reaction Prions Prions - biosynthesis Prions - chemistry Prions - genetics Prions - metabolism protein conformation Proteins Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - biosynthesis Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Sup35 protein Yeasts
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