The Region from Phenylalanine-17 to Phenylalanine-28 of a Yeast Mitochondrial ATPase Inhibitor Is Essential for Its ATPase Inhibitory Activity.
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概要
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Mitochondrial ATP synthase (F1 F0-ATPase) is regulated by an intrinsic ATPase inhibitor protein. In the present study, we investigated the structure-function relationship of the yeast ATPase inhibitor by amino acid replacement. A total of 22 mutants were isolated and characterized. Five mutants (F17S, R20G, R22G, E25A, and F28S) were entirely inactive, indicating that the residues, Phe17, Arg20, Arg22, Glu25, and Phe28, are essential for the ATPase inhibitory activity of the protein. The activity of 7 mutants (A23G, R30G, R32G, Q36G, L37G, L40S, and L44G) decreased, indicating that the residues, Ala23, Arg30, Arg32, Gln36, Leu37, Leu40, and Leu44, are also involved in the activity. Three mutants, V29G, K34Q, and K41Q, retained normal activity at pH 6.5, but were less active at pH 7.2, indicating that the residues, Val29, Lys34, and Lys41, are required for the protein's action at higher pH. The effects of 6 mutants (D26A, E35V, H39N, H39R, K46Q, and K49Q) were slight or undetectable, and the residues Asp26, Glu35, His39, Lys46, and Lys49 thus appear to be dispensable. The mutant E21A retained normal ATPase inhibitory activity but lacked pH-sensitivity. Competition experiments suggested that the 5 inactivated mutants (F17S, R20G, R22G, E25A, and F28S) could still bind to the inhibitory site on F1 F0-ATPase. These results show that the region from the position 17 to 28 of the yeast inhibitor is the most important for its activity and is required for the inhibi-tion of F1, rather than binding to the enzyme.
- 社団法人 日本生化学会の論文
著者
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Ushida Saori
Department Of Food And Nutrition Faculty Of Human Life Science Osaka City University
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Karaki Ayako
Department Of Food And Nutrition Faculty Of Human Life Science Osaka City University
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Kawabata Miho
Department Of Food And Nutrition Faculty Of Human Life Science Osaka City University
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Mizushima Mika
Department Of Food And Nutrition Faculty Of Human Life Science Osaka City University
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Ichikawa Naoki
Department Of Chemistry Graduate School Of Science Hiroshima University
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Hashimoto Tadao
Deportment of Applied Chemistry, Muroran Institute of technology.
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