Ontology highlight
ABSTRACT:
SUBMITTER: Douglas PM
PROVIDER: S-EPMC2438228 | biostudies-literature | 2008 May
REPOSITORIES: biostudies-literature
Douglas Peter M PM Treusch Sebastian S Ren Hong-Yu HY Halfmann Randal R Duennwald Martin L ML Lindquist Susan S Cyr Douglas M DM
Proceedings of the National Academy of Sciences of the United States of America 20080514 20
Protein conformational diseases are associated with the aberrant accumulation of amyloid protein aggregates, but whether amyloid formation is cytotoxic or protective is unclear. To address this issue, we investigated a normally benign amyloid formed by the yeast prion [RNQ(+)]. Surprisingly, modest overexpression of Rnq1 protein was deadly, but only when preexisting Rnq1 was in the [RNQ(+)] prion conformation. Molecular chaperones protect against protein aggregation diseases and are generally be ...[more]