Characterization of Soft Amyloid Cores in Human Prion-Like Proteins.

ABSTRACT: Prion-like behaviour is attracting much attention due to the growing evidences that amyloid-like self-assembly may reach beyond neurodegeneration and be a conserved functional mechanism. The best characterized functional prions correspond to a subset of yeast proteins involved in translation or transcription. Their conformational promiscuity is encoded in Prion Forming Domains (PFDs), usually long and intrinsically disordered protein segments of low complexity. The compositional bias of these regions seems to be important for the transition between soluble and amyloid-like states. We have proposed that the presence of cryptic soft amyloid cores embedded in yeast PFDs can also be important for their assembly and demonstrated their existence and self-propagating abilities. Here, we used an o

SUBMITTER: Batlle C 

PROVIDER: S-EPMC5608858 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature