Prion Formation and Polyglutamine Aggregation Are Controlled by Two Classes of Genes 英文参考文献.docVIP

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Prion Formation and Polyglutamine Aggregation Are Controlled by Two Classes of Genes 英文参考文献.doc

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Prion Formation and Polyglutamine Aggregation Are Controlled by Two Classes of Genes 英文参考文献

PrionFormationandPolyglutamineAggregationAre ControlledbyTwoClassesofGenes AnitaL.Manogaran1,2,JooY.Hong1,JoanHufana1,JensTyedmers3,4,SusanLindquist4,SusanW. Liebman1* 1Department of Biological Sciences, Laboratory for Molecular Biology, University of Illinois at Chicago, Chicago, Illinois, United States of America, 2Department of BiologicalSciences,University ofWisconsin-Milwaukee,Milwaukee, Wisconsin, UnitedStates ofAmerica, 3Zentrumfuer Molekulare BiologieHeidelberg, DKFZ-ZMBH- Alliance, Universitaet Heidelberg, Heidelberg, Germany, 4Whitehead Institute for Biomedical Research and Howard Hughes Medical Institute, Department of Biology, MassachusettsInstituteofTechnology,Cambridge,Massachusetts,UnitedStatesofAmerica Abstract Prions are self-perpetuating aggregated proteins that are not limited to mammalian systems but also exist in lower eukaryotes including yeast. While much work has focused around chaperones involved in prion maintenance, including Hsp104,littleisknownaboutfactorsinvolvedintheappearanceofprions.Denovoappearanceofthe[PSI ]prion,whichis + theaggregatedformoftheSup35protein,isdramaticallyenhancedbytransientoverexpressionofSUP35inthepresenceof + + the prion form of the Rnq1 protein, [PIN ]. When fused to GFP and overexpressed in [ps2] [PIN ] cells, Sup35 forms fluorescentrings,andcellswiththeseringsbudoff[PSI ]daughters.Weinvestigatedtheeffectsofover400genedeletions + + onthisdenovoinductionof[PSI ].Twoclassesofgenedeletionswereidentified.ClassIdeletions(bug1D,bem1D,arf1D, and hog1D) reduced the efficiency of [PSI ] induction, but formed rings normally. Class II deletions (las17D, vps5D , and sac6D) inhibitedboth [PSI ] inductionandring formation.Furthermore, class II deletions reduced,while class Ideletions + + enhanced, toxicity associated with the expanded glutamine repeats of the huntingtin protein exon 1 that causes Huntington’sdisease.Thissuggeststhatprionformationandpolyglutamineaggregationinvolveamulti-phaseprocessthat canb