Non-targeted identification of prions and amyloid-forming proteins from yeast and mammalian cells.

ABSTRACT: The formation of amyloid aggregates is implicated both as a primary cause of cellular degeneration in multiple human diseases and as a functional mechanism for providing extraordinary strength to large protein assemblies. The recent identification and characterization of several amyloid proteins from diverse organisms argues that the amyloid phenomenon is widespread in nature. Yet identifying new amyloid-forming proteins usually requires a priori knowledge of specific candidates. Amyloid fibers can resist heat, pressure, proteolysis, and denaturation by reagents such as urea or sodium dodecyl sulfate. Here we show that these properties can be exploited to identify naturally occurring amyloid-forming proteins directly from cell lysates. This proteomic-based approach utilizes a novel purific

SUBMITTER: Kryndushkin D 

PROVIDER: S-EPMC3779709 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature