期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 365, 期 3, 页码 773-782出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2006.10.069
关键词
amyloid-like; [PIN+]; prion; protein-only; Rnq1p
资金
- NIGMS NIH HHS [R01 GM056350-10, R01 GM056350, GM 56350] Funding Source: Medline
Prions are self-propagating, infectious protein conformations. The mammalian prion, PrPSc, responsible for neurodegenerative diseases like bovine spongiform encephalopathy (BSE; mad cow disease) and Creutzfeldt-Jakob's disease, appears to be a beta-sheet-rich amyloid conformation of PrPc that converts PrPc into PrPSc. However, an unequivocal demonstration of protein-only infection by PrPSc is still lacking. So far, protein only infection has been proven for three prions, [PSI+], [URE3] and [Het-s], all of fungal origin. Considerable evidence supports the hypothesis that another protein, the yeast Rnq1p, can form a prion, [PIN+]. While Rnq1p does not lose any known function upon prionization, [PIN+] has interesting positive phenotypes: facilitating the appearance and destabilization of other prions. as well as the aggregation of polyglutamine extensions of the Huntingtin protein. Here, we polymerize a Gln/Asn-rich recombinant fragment of Rnq1p into beta-sheet-rich amyloid-like aggregates. While the method used for [PSI+] and [URE3] infectivity assays did not yield protein-only infection for the Rnq1p aggregates, we did successfully obtain protein-only infection by modifying the protocol. This work proves that [PIN+] is a prion mediated by amyloid-like aggregates of Rnq1p, and supports the hypothesis that heterologous prions affect each other's appearance and propagation through interaction of their amyloid-like regions. (c) 2006 Published by Elsevier Ltd.
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