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Hspl04 is a highly conserved protein with two essential nucleotide-binding sites

Nature volume 353, pages 270–273 (1991)Cite this article

Abstract

MOST eukaryotic cells produce proteins with relative molecular masses in the range of 100,000 to 110,000 after exposure to high temperatures1. These proteins have been studied only in yeast and mammalian cells. In Saccharomyces cerevisiae, heat-shock protein hsp104 is vital for tolerance to heat, ethanol and other stresses (ref. 2, and Y.S. et al., manuscript submitted). The mammalian hsp110 protein is nucleolar and redistributes with growth state, nutritional conditions and heat shock3,5. The relationships between hsp110, hsp104 and the high molecular mass heat-shock proteins of other organisms were unknown. We report here that hsp104 is a member of the highly conserved ClpA/ClpB protein family first identified in Escherlchla coli6 and that additional heat-inducible members of this family are present in Schizosaccharomyces pombe and in mammals. Mutagenesis of two putative nucleotide-binding sites in hsp104 indicates that both are essential for function in thermotolerance.

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Author notes

  1. Susan Lindquist: To whom correspondence should be addressed.

Authors and Affiliations

  1. Howard Hughes Medical Institute and Department of Molecular Genetics and Cell Biology, University of Chicago, 5841 S. Maryland Avenue, Chicago, Illinois, 60637, USA

    Dawn A. Parselt, Yolanda Sanchez, Joel D. Stitzel & Susan Lindquist

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  1. Dawn A. Parselt
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  2. Yolanda Sanchez
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  3. Joel D. Stitzel
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Parselt, D., Sanchez, Y., Stitzel, J. et al. Hspl04 is a highly conserved protein with two essential nucleotide-binding sites. Nature 353, 270–273 (1991). https://doi.org/10.1038/353270a0

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