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INVESTIGATIONMutational Evaluation of Sse1 (Hsp110) Suggests an Integral Role for this Chaperone in Yeast Prion Propagation In Vivo*Yeast Genetics Laboratory and also the Marie Curie Laboratory for Membrane Proteins, Department of Biology, National University of Ireland Maynooth, Maynooth, County Kildare, Ireland, and National Laboratory of 5-HT3 Receptor Modulator Formulation Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Chaoyang District, Beijing 100101, ChinaCiara Moran,* Gemma K. Kinsella, Zai-Rong Zhang,,1 Sarah Perrett, and Gary W. Jones*,ABSTRACT The yeast Hsp110 chaperone Sse1 is really a conserved protein that’s a noncanonical member of the Hsp70 protein superfamily. Sse1 influences the cellular response to heat strain and has also been implicated in playing a role within the propagation of prions in yeast. Sse1 can seemingly exert its effects in vivo through direct or indirect actions by influencing the nucleotide exchange activity of canonical cytosolic Hsp70s. Applying a genetic screen based on the inability to propagate the yeast [PSI+] prion, we have identified 13 new Sse1 mutants which are predicted to alter chaperone function through various different mechanisms. Not simply are these new Sse1 mutants altered within the ability to propagate and cure yeast prions but P2Y6 Receptor Molecular Weight additionally to varying degrees within the ability to grow at elevated temperatures. The expression levels of chaperone proteins recognized to influence yeast prion propagation are unaltered in the Sse1 mutants, suggesting that the observed phenotypic.