Work

Pernicious Pathogens or Expedient Elements of Inheritance: The Significance of Yeast Prions

Year: 2014

Type: review

Abstract: Prions are ‘‘infectious’ ’ misfolded protein states that can template their self-perpetuating conformations onto other mole-cules of the same type. This unusual folding landscape drives a paradigm-shifting mechanism of inheritance based on changes in protein conformation rather than changes in nucleic acid. The first prion discovered, Prion Protein (PrP), is the causal agent of several human neurodegenerative diseases, including kuru and Creutz-feldt-Jakob [1]. This history has engendered the widespread perception that prions are inherently pathogenic. However, many additional prions have now been found in other eukaryotes in which they influence diverse biological processes and can produce beneficial traits. The most well-characterized of these are found in Saccharomyces cerevisiae and other fungi, such as Podospora anserina [2]. The best-studied prion is the yeast translation termination factor Sup35. In its soluble form, this protein promotes the faithful

Source: PLoS Pathogens

DOI: 10.1371/journal.ppat.1003992

Authors: James S. Byers, Daniel F. Jarosz

Institutions: Stanford Medicine, Stanford University

Language: English

Topic: Prion Diseases and Protein Misfolding

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $3,043

Funders: National Institutes of Health, National Institute of General Medical Sciences