Distinct type of transmission barrier revealed by study of multiple prion determinants of Rnq1.

ABSTRACT: Prions are self-propagating protein conformations. Transmission of the prion state between non-identical proteins, e.g. between homologous proteins from different species, is frequently inefficient. Transmission barriers are attributed to sequence differences in prion proteins, but their underlying mechanisms are not clear. Here we use a yeast Rnq1/[PIN(+)]-based experimental system to explore the nature of transmission barriers. [PIN(+)], the prion form of Rnq1, is common in wild and laboratory yeast strains, where it facilitates the appearance of other prions. Rnq1's prion domain carries four discrete QN-rich regions. We start by showing that Rnq1 encompasses multiple prion determinants that can independently drive amyloid formation in vitro and transmit the [PIN(+)] prion state in vivo.

SUBMITTER: Kadnar ML 

PROVIDER: S-EPMC2809767 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature