Similar dose response of heat shock protein synthesis and intracellular pH change in yeast

doi:10.1016/S0014-4827(85)80054-9

Experimental Cell Research

Volume 159, Issue 1, July 1985, Pages 252-256

https://doi.org/10.1016/S0014-4827(85)80054-9 Get rights and content

In Saccharomyces cerevisiae both the induction of heat shock proteins (98, 85, 70 kD) and the intracellular pH, determined by means of ³¹P-NMR spectroscopy, show a similar dose response to increasing temperature or concentrations of 2,4-dinitrophenol (DNP). Temperature increases from 23° to 32°C or more, or concentrations of DNP higher than 1 mM cause a significant increase in the synthesis rate of heat shock proteins and a significant decrease of the intracellular pH. A similar correlation is found in a mitochondrial mutant (ϱ⁰) defective in oxidative phosphorylation. Intracellular signal transduction may thus involve H⁺-concentration changes independent of intact oxidative phosphorylation.

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Although the condensates formed at low pH were spherical, condensates formed at elevated temperature resembled clusters of small spherical structures, suggesting that they form by phase separation but then gel rapidly. Heat-shocked cells experience a decrease in cytosolic pH to approximately 6.5 (Kroschwald et al., 2018; Weitzel et al., 1985). We thus tested for the effect of pH on temperature-induced Ded1p condensation.
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It is well known that HSP72, the inducible form of HSP70, is up-regulated by exposure to heat [9,10,16,17]. Up-regulation of HSP72 is induced by not only heat-stress but also many types of cellular stresses, such as the reduced peripheral blood circulation, oxygen radicals, and/or H+[9,18–21]. The HSP72 function as an important molecular chaperone [22,23].
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Short NoteSimilar dose response of heat shock protein synthesis and intracellular pH change in yeast

Cell

Exp cell res

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Current genet

Nature

Subcell biochem

Short Note
Similar dose response of heat shock protein synthesis and intracellular pH change in yeast