Search Organism: All OrganismsArabidopsis thalianaBacillus subtilis 168Bos taurusCaenorhabditis elegansCanis familiarisDanio rerioDrosophila melanogasterEquus caballusEscherichia coli K12Gallus gallusHomo sapiensMacaca mulattaMus musculusNematostella vectensisOryza sativaPan troglodytesRattus norvegicusSaccharomyces cerevisiaeSchizosaccharomyces pombeStrongylocentrotus purpuratusTakifugu rubripesXenopus laevis home help / support contribute downloads mirrors about us Mol. Biol. Cell Jun (2008); 19(6):2433-43 Variant-specific [PSI-] infection is transmitted by Sup35 polymers within [PSI-] aggregates with heterogeneous protein composition- Bagriantsev SN, Gracheva EO, Richmond JE, Liebman SW Department of Biological Sciences, University of Illinois at Chicago, Chicago, IL 60607, USA- Abstract: The [PSI---] prion is the aggregated self-propagating form of the Sup35 protein from the yeast Saccharomyces cerevisiae- Aggregates of Sup35 in [PSI---] cells exist in different heritable conformations, called "variants," and they are composed of detergent-resistant Sup35 polymers, which may be closely associated with themselves, other proteins, or both- Here, we report that disassembly of the aggregates into individual Sup35 polymers and non-Sup35 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 seem 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 that it interacts poorly with the nonaggregated Sup35 found in [psi---] cells- Hsp104, Sis1, and Sse1 interact preferentially with the prion versus nonprion form of Sup35, whereas Sla2 and Ssb1-2 interact with both forms of Sup35 with similar efficiency- [PUBMED: 18353968] Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. terms and conditions - privacy policy - Osprey Network Visualization System BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9.