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    Mutational Analysis of Sse1 (Hsp110) Suggests an Integral Role for this Chaperone in Yeast Prion Propagation In Vivo


    Moran, Ciara and Kinsella, Gemma K. and Zhang, Zai-Rong and Perrett, Sarah and Jones, Gary W. (2013) Mutational Analysis of Sse1 (Hsp110) Suggests an Integral Role for this Chaperone in Yeast Prion Propagation In Vivo. G3. ISSN 2160-1836

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    Abstract

    The yeast Hsp110 chaperone Sse1 is a conserved protein that is a non-canonical member of the Hsp70 protein super-family. Sse1 influences the cellular response to heat stress and has also been implicated in playing a role in 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. Using a genetic screen based on the inability to propagate the yeast [PSI+] prion, we have identified thirteen new Sse1 mutants that are predicted to alter chaperone function through a variety of different mechanisms. Not only are these new Sse1 mutants altered in the ability to propagate and cure yeast prions but also to varying degrees in the ability to grow at elevated temperatures. The expression levels of chaperone proteins known to influence yeast prion propagation are unaltered in the Sse1 mutants suggesting that the observed phenotypic effects are due to direct functional alterations in these mutants. Mapping the location of the mutants onto the Sse1 crystal structure suggests that more than one functional alteration in Sse1 may result in changes in prion propagation and ability to function at elevated temperatures. All Sse1 mutants isolated provide essential functions in the cell under normal growth conditions, thus further demonstrating that essential chaperone functions in vivo can to some degree at least be detached from those related to propagation of prions. Our results suggest that Sse1 can influence prion propagation through a variety of different mechanisms.

    Item Type: Article
    Keywords: Saccharomyces cerevisiae; Hsp110; Sse1; chaperone; prion;
    Academic Unit: Faculty of Science and Engineering > Biology
    Item ID: 4488
    Depositing User: Dr. Gary Jones
    Date Deposited: 16 Sep 2013 13:25
    Journal or Publication Title: G3
    Publisher: Genetics Society of America
    Refereed: Yes
    URI:

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