Abstract
Exposure of cells or tissues of various living organisms to elevated temperatures induces the synthesis of a family of specific proteins called heat-shock proteins (HSPs)1–3. This phenomenon has so far been investigated mostly with respect to the induction mechanism of these HSPs4,5. However, little is known about the function of such proteins, although it has been suggested that they are involved in the acquisition of thermal tolerance3. We have recently suggested that a specific class of HSPs may function as negatively regulatory molecules in the growth of eukaryotic cells6–8, and that a HSP of relative molecular mass (Mr) 48,000 (HSP48) from the yeast Saccharomyces cerevisiae may be involved in both thermal tolerance and growth control in this organism8. We now present evidence that S. cerevisiae HSP48 is an isoprotein of a glycolytic enzyme, enolase (EC 4.2.1.11). This unexpected finding may provide new insight into the role of the protein in the acquisition of thermal tolerance and growth control.
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Iida, H., Yahara, I. Yeast heat-shock protein of Mr 48,000 is an isoprotein of enolase. Nature 315, 688–690 (1985). https://doi.org/10.1038/315688a0
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DOI: https://doi.org/10.1038/315688a0
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