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Hsp30, the integral plasma membrane heat shock protein of Saccharomyces cerevisiae, is a stress-inducible regulator of plasma membrane H+-ATPase.

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P Piper, C Ortiz-Calderon, C Holyoak, Peter John Coote, M Cole

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Saccharomyces cerevisiae has a single integral plasma membrane heat shock protein (Hsp). This Hsp30 is induced by several stresses, including heat shock, ethanol exposure, severe osmostress, weak organic acid exposure and glucose limitation. Plasma membrane H+-ATPase activities of heat shocked and weak acid-adapted, hsp30 mutant and wild-type cells, revealed that Hsp30 induction leads to a downregulation of the stress-stimulation of this H+-ATPase. Plasma membrane H+-ATPase activity consumes a substantial fraction of the ATP generated by the cell, a usage that will be increased by the H+-ATPase stimulation occurring with several Hsp30-inducing stresses. Hsp30 might therefore provide an energy conservation role, limiting excessive ATP consumption by plasma membrane H+-ATPase during prolonged stress exposure or glucose limitation. Consistent with the role of Hsp30 being energy conservation, Hsp30 null cultures give lower final biomass yields. They also have lower AIP levels, consistent with higher H+-ATPase activity, at the glucose exhaustion stage of batch fermentations (diauxic lag), when Hsp30 is normally induced. Loss of Hsp30 does not affect several stress tolerances but it extends the time needed for cells to adapt to growth under several stressful conditions where the maintenance of homeostasis will demand an unusually high usage of energy. hsp30 is the first yeast gene identified as both weak organic acid-inducible and assisting the adaptation to growth in the presence of these acids.



Original languageEnglish
Pages (from-to)12-24
Number of pages13
JournalCell Stress and Chaperones
Issue number1
Publication statusPublished - Mar 1997

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