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- W2143487009 abstract "The structure of the F0 part of ATP synthases from E. coli and Neurospora crassa was analyzed by hydrophobic surface labeling with [125I]TID. In the E. coli F0 all three subunits were freely accessible to the reagent, suggesting that these subunits are independently integrated in the membrane. Labeled amino acid residues were indentified by Edman degradation of the dicyclohexylcarbodiimide binding (DCCD) proteins from E. coli and Neurospora crassa. The very similar patterns obtained with the two homologous proteins suggested the existence of tightly packed α-helices. The oligomeric structure of the DCCD binding protein appeared to be very rigid since little, if any, change in the labeling pattern was observed upon addition of oligomycin or DCCD to membranes from Neurospora crassa. When membranes were pretreated with DCCD prior to the reaction with [125I]TID an additionally labeled amino acid appeared at the position of Glu-65 which binds DCCD covalently, indicating the location of this inhibitor on the outside of the oligomer. It is suggested that proton conduction occurs at the surface of the oligomer of the DCCD binding protein. Possibly this oligomer rotates against the subunit a or b and thus enables proton translocation. Conserved residues in subunit a, probably located in the lipid bilayer, might participate in the proton translocation mechanism. La structure de la partie F0 de l'ATP synthase a été analysée au moyen de marquage par le réactif hydrophobe TID[125I]. Les trois sous-unités de E. coli F0 sont accessibles au réactif ce qui semble indiquer que ces sous-unités sont intégrées dans la membrane de façon indépendante. Les amino-acides marqués ont été identifiés par la dégradation d'Edman des protéines d'E. coli et de Neurospora associées au dicyclohexylcarbodiimide (DCCD). L'analogie des courbes obtenues pour les deux protéines homologues suggère l'existence d'α-hélices rangées de façon serrée. La structure oligomérique de la protéine associée au DCCD semble être très rigide puisque pratiquement aucun changement dans le marquage n'a été observé par addition d'oligomycine ou de DCCD aux membranes de Neurospora crassa. Quand les membranes sont traitées avec le DCCD avant la réaction avec TID[125I], un amino-acide additionnellement marqué apparaît à la position Glu-65 et forme avec le DCCD une liaison covalente. Ce dernier résultat indique la localisation de cet inhibiteur à l'extérieur de l'oligomère. Il semble donc que la conduction des protons ait lieu à la surface de l'oligomère de la protéine associée au DCCD. Il serait possible que l'oligomère se retourne contre la sous-unité a ou b, permettant de ce fait la translocation des protons. Les résidus conservés de la sous-unité a, probablement localisés dans la double couche lipidique, pourraient participer au mécanisme de translocation des protons." @default.
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- W2143487009 date "1986-03-01" @default.
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- W2143487009 title "Topological studies suggest that the pathway of the protons through F0 is provided by amino acid residues accessible from the lipid phase" @default.
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- W2143487009 doi "https://doi.org/10.1016/s0300-9084(86)80010-4" @default.
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