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Genetika ; 50(3): 273-81, 2014 Mar.
Artigo em Russo | MEDLINE | ID: mdl-25438547

RESUMO

The elevation of Hsp104 (heat shock protein) content under heat shock plays a key role in yeast (Saccharomyces cerevisiae) cells. Hsp104 synthesis is increased under heat stress in the stationary growth phase. As shown, the loss of mitochondrial DNA (petite mutation) inhibited the induction of the Hsp104 synthesis under heat stress (39 degrees C) during the transition to the stationary growth phase. Also, the petite mutation suppressed the activity of antioxidant enzymes in the same phase, which led to lower thermotolerance. At the same time, the mutation inhibited production of the reactive oxygen species and prevented cell death under heat shock in the logarithmic growth phase. The results of this study suggest that disruption of the mitochondrial functional state suppresses the expression level of yeast nuclear genes upon transitioning to the stationary growth phase.


Assuntos
DNA Mitocondrial/genética , Proteínas de Choque Térmico/metabolismo , Proteínas de Saccharomyces cerevisiae/metabolismo , Saccharomyces cerevisiae/metabolismo , Deleção de Genes , Proteínas de Choque Térmico/biossíntese , Proteínas de Choque Térmico/genética , Resposta ao Choque Térmico , Espécies Reativas de Oxigênio/metabolismo , Fase S , Saccharomyces cerevisiae/genética , Saccharomyces cerevisiae/fisiologia , Proteínas de Saccharomyces cerevisiae/biossíntese , Proteínas de Saccharomyces cerevisiae/genética
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