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• W2126828350 abstract "Research Article1 January 1983free access The topology of the proton translocating F0 component of the ATP synthase from E. coli K12: studies with proteases. J. Hoppe J. Hoppe Department of Stoffwechselregulation, GBF-Gesellschaft für Biotechnologische Forschung mbH., Braunschweig-Stöckheim, FRG. Search for more papers by this author P. Friedl P. Friedl Department of Stoffwechselregulation, GBF-Gesellschaft für Biotechnologische Forschung mbH., Braunschweig-Stöckheim, FRG. Search for more papers by this author H.U. Schairer H.U. Schairer Department of Stoffwechselregulation, GBF-Gesellschaft für Biotechnologische Forschung mbH., Braunschweig-Stöckheim, FRG. Search for more papers by this author W. Sebald W. Sebald Department of Stoffwechselregulation, GBF-Gesellschaft für Biotechnologische Forschung mbH., Braunschweig-Stöckheim, FRG. Search for more papers by this author K. von Meyenburg K. von Meyenburg Department of Stoffwechselregulation, GBF-Gesellschaft für Biotechnologische Forschung mbH., Braunschweig-Stöckheim, FRG. Search for more papers by this author B.B. Jørgensen B.B. Jørgensen Department of Stoffwechselregulation, GBF-Gesellschaft für Biotechnologische Forschung mbH., Braunschweig-Stöckheim, FRG. Search for more papers by this author J. Hoppe J. Hoppe Department of Stoffwechselregulation, GBF-Gesellschaft für Biotechnologische Forschung mbH., Braunschweig-Stöckheim, FRG. Search for more papers by this author P. Friedl P. Friedl Department of Stoffwechselregulation, GBF-Gesellschaft für Biotechnologische Forschung mbH., Braunschweig-Stöckheim, FRG. Search for more papers by this author H.U. Schairer H.U. Schairer Department of Stoffwechselregulation, GBF-Gesellschaft für Biotechnologische Forschung mbH., Braunschweig-Stöckheim, FRG. Search for more papers by this author W. Sebald W. Sebald Department of Stoffwechselregulation, GBF-Gesellschaft für Biotechnologische Forschung mbH., Braunschweig-Stöckheim, FRG. Search for more papers by this author K. von Meyenburg K. von Meyenburg Department of Stoffwechselregulation, GBF-Gesellschaft für Biotechnologische Forschung mbH., Braunschweig-Stöckheim, FRG. Search for more papers by this author B.B. Jørgensen B.B. Jørgensen Department of Stoffwechselregulation, GBF-Gesellschaft für Biotechnologische Forschung mbH., Braunschweig-Stöckheim, FRG. Search for more papers by this author Author Information J. Hoppe1, P. Friedl1, H.U. Schairer1, W. Sebald1, K. Meyenburg1 and B.B. Jørgensen1 1Department of Stoffwechselregulation, GBF-Gesellschaft für Biotechnologische Forschung mbH., Braunschweig-Stöckheim, FRG. The EMBO Journal (1983)2:105-110https://doi.org/10.1002/j.1460-2075.1983.tb01389.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info The accessibility of the three F0 subunits a, b and c from the Escherichia coli K12 ATP synthase to various proteases was studied in F1-depleted inverted membrane vesicles. Subunit b was very sensitive to all applied proteases. Chymotrypsin produced a defined fragment of mol. wt. 15,000 which remained tightly bound to the membrane. The cleavage site was located at the C-terminal region of subunit b. Larger amounts of proteases were necessary to attack subunit a (mol. wt. 30,000). There was no detectable cleavage of subunit c. It is suggested that the major hydrophilic part of subunit b extends from the membrane into the cytoplasm and is in contact with the F1 sector. The F1 sector was found to afford some protection against proteolysis of the b subunit in vitro and in vivo. Protease digestion had no influence on the electro-impelled H+ conduction via F0 but ATP-dependent H+ translocation could not be reconstituted upon binding of F1. A possible role for subunit b as a linker between catalytic events on the F1 component and the proton pathway across the membrane is discussed. Previous ArticleNext Article Volume 2Issue 11 January 1983In this issue RelatedDetailsLoading ..." @default.
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• W2126828350 title "The topology of the proton translocating F0 component of the ATP synthase from E. coli K12: studies with proteases." @default.
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