Báo cáo khoa học: The transmembrane domain of subunitbof theEscherichia coli F1FOATP synthase is sufficient for H + -translocating activity together with subunitsaandc
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Subunitbis indispensable for the formation of a functionalH+-translocating FOcomplex both in vivo andin vitro.Whereas the very C-terminus of subunitbinteracts with F1and plays a crucial role in enzyme assembly, the C-terminalregion is also considered to be necessary for proper recon-stitution of FOinto liposomes. Here, we show that a syn-thetic peptide, residues 1–34 of subunitb(b1)34) [Dmitriev,O., Jones, P.C., Jiang,W. & Fillingame, R.H. (1999)J. Biol.Chem.274, 15598–15604], corresponding to the membranedomain of subunitbwas sufficient in forming an active FOcomplex when coreconstitutedwith purifiedacsubcomplex....
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Báo cáo khoa học: The transmembrane domain of subunitbof theEscherichia coli F1FOATP synthase is sufficient for H + -translocating activity together with subunitsaandc
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Báo cáo khoa học: The transmembrane domain of subunitbof theEscherichia coli F1FOATP synthase is sufficient for H + -translocating activity together with subunitsaandc
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