Fedoseeva I V, Rikhanov E G, Varakina N N, Rusaleva T M, Pyatrikas D V, Stepanov A V, Fedyaeva A V
Genetika. 2014 Mar;50(3):273-81.
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.
热休克条件下Hsp104(热休克蛋白)含量的升高在酵母(酿酒酵母)细胞中起关键作用。在稳定生长期的热应激条件下,Hsp104的合成增加。如图所示,线粒体DNA的缺失(小菌落突变)抑制了向稳定生长期转变过程中热应激(39摄氏度)条件下Hsp104合成的诱导。此外,小菌落突变在同一时期抑制了抗氧化酶的活性,导致耐热性降低。同时,该突变抑制了活性氧的产生,并防止对数生长期细胞在热休克条件下死亡。本研究结果表明,线粒体功能状态的破坏在向稳定生长期转变时会抑制酵母核基因的表达水平。