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• W2155842009 abstract "ABSTRACT We have recently reported that the yeast chromatin-remodeling factor Swi1 can exist as a prion, [ SWI + ], demonstrating a link between prionogenesis and global transcriptional regulation. To shed light on how the Swi1 conformational switch influences Swi1 function and to define the sequence and structural requirements for [ SWI + ] formation and propagation, we functionally dissected the Swi1 molecule. We show here that the [ SWI + ] prion features are solely attributable to the first 327 amino acid residues (N), a region that is asparagine rich. N was aggregated in [ SWI + ] cells but diffuse in [ swi − ] cells; chromosomal deletion of the N-coding region resulted in [ SWI + ] loss, and recombinant N peptide was able to form infectious amyloid fibers in vitro , enabling [ SWI + ] de novo formation through a simple transformation. Although the glutamine-rich middle region (Q) was not sufficient to aggregate in [ SWI + ] cells or essential for SWI/SNF function, it significantly modified the Swi1 aggregation pattern and Swi1 function. We also show that excessive Swi1 incurred Li + /Na + sensitivity and that the N/Q regions are important for this gain of sensitivity. Taken together, our results provide the final proof of “protein-only” transmission of [ SWI + ] and demonstrate that the widely distributed “dispensable” glutamine/asparagine-rich regions/motifs might have important and divergent biological functions." @default.
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• W2155842009 creator A5069507396 @default.
• W2155842009 date "2010-10-01" @default.
• W2155842009 modified "2023-10-13" @default.
• W2155842009 title "Distinct Subregions of Swi1 Manifest Striking Differences in Prion Transmission and SWI/SNF Function" @default.
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• W2155842009 doi "https://doi.org/10.1128/mcb.00225-10" @default.
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