[Induction of synthesis of Hsp104 of Saccharomyces cerevisiae in heat shock is controlled by mitochondria].
Heat shock protein Hsp104 of Saccharomyces cerevisiae functions as a protector of cells against heat stress. When yeast are grown in media containing nonfermentable carbon sources, the constitutive level of this protein increases, which suggests an association between the expression of Hsp104 and yeast energy metabolism. In this work, it is shown that distortions in the function of mitochondria appearing as a result of mutation petite or after exposure of cells to the mitochondrial inhibitor sodium azide reduce the induction of Hsp104 synthesis during heat shock. Since the addition of sodium azide suppressed the formation of induced thermotolerance in the parent type and in mutant hsp104, the expression of gene HSP104 and other stress genes during heat shock is apparently regulated by mitochondria.
Rikhvanov
E G
EG
Siberian Institute of Cytology and Genetics, Russian Academy of Sciences, Irkutsk, 664033 Russia.
Rachenko
E I
EI
Varakina
N N
NN
Rusaleva
T M
TM
Borovskiĭ
G B
GB
Voĭnikov
V K
VK
D006360:Heat-Shock Proteins / Q000096:biosynthesis / Q000235:genetics*; D018869:Heat-Shock Response; D008928:Mitochondria / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins / Q000096:biosynthesis / Q000235:genetics*
D006360:Heat-Shock Proteins; D029701:Saccharomyces cerevisiae Proteins; C070972:HsP104 protein, S cerevisiae