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• W1570668744 abstract "A set of mutants of the Escherichia coli F1F0-type ATPase has been generated by site-directed mutagenesis as follows: βE381C, βS383C, βE381C/εS108C, and βS383C/εS108C. Treatment of ECF1isolated from any of these mutants with CuCl2induces disulfide bond formation. For the single mutants, βE381C and βS383C, a disulfide bond is formed in essentially 100% yield between a β subunit and the γ subunit, probably at Cys87based on the recent structure determination of F1(Abrahams, J. P., Leslie, A. G. W., Lutter, R., and Walker, J. E. (1994) Nature 370, 621-628). In the double mutants, two [Medline] disulfide bonds are formed, again in essentially full yield, one between β and γ, the other between a β and the ε subunit via Cys108. The same two cross-links are produced with CuCl2treatment of ECF1F0isolated from either of the double mutants. These results show that the parts of γ around residue 87 (a short α-helix) and the ε subunit interact with different β subunits.The yield of covalent linkage of β to γ is nucleotide dependent and highest in ATP and much lower with ADP in catalytic sites. The yield of covalent linkage of β to ε is also nucleotide dependent but in this case is highest in ADP and much lower in ATP. Disulfide bond formation between either β and γ, or β and ε inhibits the ATPase activity of the enzyme in proportion to the yield of the cross-linked product. Chemical modification of the Cys at either position 381 or 383 of the β subunit inhibits ATPase activity in a manner that appears to be dependent on the size of the modifying reagent. These results are as expected if movements of the catalytic site-containing β subunits relative to the γ and ε subunits are an essential part of the cooperativity of the enzyme. A set of mutants of the Escherichia coli F1F0-type ATPase has been generated by site-directed mutagenesis as follows: βE381C, βS383C, βE381C/εS108C, and βS383C/εS108C. Treatment of ECF1isolated from any of these mutants with CuCl2induces disulfide bond formation. For the single mutants, βE381C and βS383C, a disulfide bond is formed in essentially 100% yield between a β subunit and the γ subunit, probably at Cys87based on the recent structure determination of F1(Abrahams, J. P., Leslie, A. G. W., Lutter, R., and Walker, J. E. (1994) Nature 370, 621-628). In the double mutants, two [Medline] disulfide bonds are formed, again in essentially full yield, one between β and γ, the other between a β and the ε subunit via Cys108. The same two cross-links are produced with CuCl2treatment of ECF1F0isolated from either of the double mutants. These results show that the parts of γ around residue 87 (a short α-helix) and the ε subunit interact with different β subunits. The yield of covalent linkage of β to γ is nucleotide dependent and highest in ATP and much lower with ADP in catalytic sites. The yield of covalent linkage of β to ε is also nucleotide dependent but in this case is highest in ADP and much lower in ATP. Disulfide bond formation between either β and γ, or β and ε inhibits the ATPase activity of the enzyme in proportion to the yield of the cross-linked product. Chemical modification of the Cys at either position 381 or 383 of the β subunit inhibits ATPase activity in a manner that appears to be dependent on the size of the modifying reagent. These results are as expected if movements of the catalytic site-containing β subunits relative to the γ and ε subunits are an essential part of the cooperativity of the enzyme." @default.
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• W1570668744 date "1995-04-01" @default.
• W1570668744 modified "2023-09-28" @default.
• W1570668744 title "Disulfide Bond Formation between the COOH-terminal Domain of the β Subunits and the γ and ε Subunits of the Escherichia coli F1-ATPase" @default.
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• W1570668744 doi "https://doi.org/10.1074/jbc.270.16.9185" @default.
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