Abstract
Our laboratory recently reported a novel prion [SWI+], in the budding yeast Saccharomyces cerevisiae. [SWI+] is the prion form of Swi1, a component of the SWI/SNF chromatin-remodeling complex. Cells harboring [SWI+] exhibit a partial loss-of-function phenotype for SWI/SNF, which can be easily assayed by poor growth on some non-fermentable carbon sources such as raffinose. Swi1 is unique among yeast prion proteins for its nuclear localization and the fact that it comprises part of a large, multi-subunit protein complex. The discovery of [SWI+] demonstrates for the first time a link between prion function and chromatin remodeling, implying a possible role for prions in gene regulation. We believe that the unique features of this novel yeast prion will provide new insight into prion biology.
Figures and Tables
Figure 1 Amino acid sequences of prion domains of known prions. Asparagine (N) residues are highlighted in blue, glutamine (Q) residues are highlighted in purple, and serine (S), tyrosine (Y) and threonine (T) are highlighted in red. Underlined areas indicate the imperfect oligopeptide repeats in Sup35 and Rnq1.
![Figure 1 Amino acid sequences of prion domains of known prions. Asparagine (N) residues are highlighted in blue, glutamine (Q) residues are highlighted in purple, and serine (S), tyrosine (Y) and threonine (T) are highlighted in red. Underlined areas indicate the imperfect oligopeptide repeats in Sup35 and Rnq1.](/cms/asset/d983cf08-ec79-4e7e-ab6a-21189fe22039/kprn_a_10908069_f0001.gif)
Table 1 Percentage of amino acids present in prion domains of known yeast prions
Table 2 Swi1 is unique among yeast prions proteins due to its nuclear localization and low cellular abundance