A small, glutamine-free domain propagates the [SWI+] prion in budding yeast

Emily T. Crow, Zhiqiang Du, Liming Li*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

Yeast prions are self-propagating protein conformations that transmit heritable phenotypes in an epigenetic manner. The recently identified yeast prion [SWI +] is an alternative conformation of Swi1, a component of the evolutionarily conserved SWI/SNF chromatin-remodeling complex. Formation of the [SWI +] prion results in a partial loss-of-function phenotype for Swi1. The amino-terminal region of Swi1 is dispensable for its normal function but is required for [SWI +] formation and propagation; however, the precise prion domain (PrD) of Swi1 has not been elucidated. Here, we define the minimal Swi1 PrD as the first 37 amino acids of the protein. This region is extremely asparagine rich but, unexpectedly, contains no glutamine residues. This unusually small prion domain is sufficient for aggregation, propagation, and transmission of the [SWI +] prion. Because of its unusual size and composition, the Swi1 prion domain defined here has important implications for describing and identifying novel prions.

Original languageEnglish (US)
Pages (from-to)3436-3444
Number of pages9
JournalMolecular and cellular biology
Volume31
Issue number16
DOIs
StatePublished - Aug 2011

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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