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Titolo:
Involvement of mitochondrial aldehyde dehydrogenase ALD5 in maintenance ofthe mitochondrial electron transport chain in Saccharomyces cerevisiae
Autore:
Kurita, O; Nishida, Y;
Indirizzi:
Mie Ind Res Inst, Tsu, Mie 5140819, Japan Mie Ind Res Inst Tsu Mie Japan 5140819 Res Inst, Tsu, Mie 5140819, Japan Food Res Inst Aichi Prefectural Govt, Nishi Ku, Nagoya, Aichi 4510083, Japan Food Res Inst Aichi Prefectural Govt Nagoya Aichi Japan 4510083 83, Japan
Titolo Testata:
FEMS MICROBIOLOGY LETTERS
fascicolo: 2, volume: 181, anno: 1999,
pagine: 281 - 287
SICI:
0378-1097(199912)181:2<281:IOMADA>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACETALDEHYDE DEHYDROGENASE; MOLECULAR-CLONING; LACZ FUSIONS; YEAST; STRESS; GENE; DISRUPTION; DEFICIENT; SHUTTLE; VECTORS;
Keywords:
Saccharomyces cerevisiae; aldehyde dehydrogenase; mitochondrion; electron transport chain;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
22
Recensione:
Indirizzi per estratti:
Indirizzo: Kurita, O Mie Ind Res Inst, 5-5-45 Takajaya, Tsu, Mie 5140819, Japan Mie Ind Res Inst 5-5-45 Takajaya Tsu Mie Japan 5140819 19, Japan
Citazione:
O. Kurita e Y. Nishida, "Involvement of mitochondrial aldehyde dehydrogenase ALD5 in maintenance ofthe mitochondrial electron transport chain in Saccharomyces cerevisiae", FEMS MICROB, 181(2), 1999, pp. 281-287

Abstract

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 dehydrogenaseactivity 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 beta-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: butshowed improved growth on ethanol. These observations show that mitochondrial ALD5 plays a role in regulation or biosynthesis of electron transport chain components. (C) 1999 Federation of European Microbiological Societies. Published by Elsevier Science B.V. Ali rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/01/20 alle ore 21:00:46