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.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
Du Z,Crow ET,Kang HS,Li Ldoi
10.1128/MCB.00225-10subject
Has Abstractpub_date
2010-10-01 00:00:00pages
4644-55issue
19eissn
0270-7306issn
1098-5549pii
MCB.00225-10journal_volume
30pub_type
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