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MBC in Press, published online ahead of print March 19, 2008
Mol. Biol. Cell 10.1091/mbc.E08-01-0078

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Submitted on January 25, 2008
Revised on February 20, 2008
Accepted on March 10, 2008

Variant-specific [PSI+] Infection is Transmitted by Sup35 Polymers within [PSI+] Aggregates with Heterogeneous Protein Composition

Sviatoslav N. Bagriantsev, Elena O. Gracheva, Janet E. Richmond, and Susan W. Liebman

Department of Biological Sciences, University of Illinois at Chicago, Chicago, IL, 60607

Monitoring Editor: Jonathan Weissman

The [PSI+] prion is the aggregated self-propagating form of the Sup35 protein from the yeast S. cerevisiae. Aggregates of Sup35 in [PSI+] cells exist in different heritable conformations, called ‘variants’, and are composed of detergent-resistant Sup35 polymers, which may be closely associated with themselves and/or other proteins. Here we report that disassembly of the aggregates into individual Sup35 polymers and nonSup35 components increases their infectivity while retaining their variant-specificity, showing that variant-specific [PSI+] infection can be transmitted by Sup35 polymers alone. Morphological analysis revealed that Sup35 isolated from [PSI+] yeast has the appearance of short barrels, and bundles, which appear to be composed of barrels. We show that the major components of two different variants of [PSI+] are interacting infectious Sup35 polymers and Ssa1/2. Using a candidate approach, we detected Hsp104, Ssb1/2, Sis1, Sse1, Ydj1, and Sla2 among minor components of the aggregates. We demonstrate that Ssa1/2 efficiently binds to the prion domain of Sup35 in [PSI+] cells, but interacts poorly with the nonaggregated Sup35 found in [psi-] cells. Hsp104, Sis1, and Sse1 interact preferentially with the prion versus nonprion form of Sup35, while Sla2 and Ssb1/2 interact with both forms of Sup35 with similar efficiency.

Address correspondence to: Susan W. Liebman (sueL{at}uic.edu)






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