Open AccessInvolvement of mitochondrial aldehyde dehydrogenase ALD5 in maintenance of the mitochondrial electron transport chain in Saccharomyces cerevisiae
Author(s) -
Kurita Osamu,
Nishida Yoshio
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb08856.x
Subject(s) - aldehyde dehydrogenase , biochemistry , aldh2 , mutant , saccharomyces cerevisiae , glycerol 3 phosphate dehydrogenase , mitochondrion , respiratory chain , dehydrogenase , mitochondrial respiratory chain , branched chain alpha keto acid dehydrogenase complex , biology , nadh dehydrogenase , alcohol dehydrogenase , microbiology and biotechnology , chemistry , enzyme , mitochondrial dna , yeast , gene
The physiological role of mitochondrial aldehyde dehydrogenase ( ALD5 ) was investigated by analysis of the ald5 mutant (AKD321) in Saccharomyces cerevisiae . K + ‐activated ALDH activity of the ald5 mutant was about 80% of the wild‐type in the mitochondrial fraction, while the respiratory activity of the ald5 mutant was greatly reduced. Cytochrome content was also reduced in the ald5 mutant. Enzymatic analysis revealed that the alcohol dehydrogenase activity of the ald5 mutant was higher than that of the wild‐type, while glycerol 3‐phosphate dehydrogenase activity was the same in the two strains. Ethanol as a carbon source or addition of 1 M NaCl with glucose as the carbon source in the growth medium increased β‐galactosidase activity from an ALD5‐lacZ fusion. Overexpression of another mitochondrial ALDH gene ( ALD7 ) had no effect on increasing respiratory function of the ald5 mutant, but showed improved growth on ethanol. These observations show that mitochondrial ALD5 plays a role in regulation or biosynthesis of electron transport chain components.