Direct interaction of subunits a and b of the F-0 complex of Escherichia coli ATP synthase by forming an ab(2) subcomplex

Autor(en): Stalz, WD
Greie, JC
Deckers-Hebestreit, G 
Altendorf, K 
Stichwörter: ADENOSINE-TRIPHOSPHATASE; Biochemistry & Molecular Biology; C OLIGOMER; CROSS-LINKING; F1F0; MECHANISM; MEMBRANE MOIETY; ORGANIZATION; PROTON-TRANSLOCATING ATPASE; RECONSTITUTION; ROTARY MOTOR
Erscheinungsdatum: 2003
Herausgeber: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Journal: JOURNAL OF BIOLOGICAL CHEMISTRY
Volumen: 278
Ausgabe: 29
Startseite: 27068
Seitenende: 27071
Zusammenfassung: 
The addition of a His(6) tag to the N terminus of subunit a of the F-0 complex of the Escherichia coli ATP synthase allowed the purification of an ab(2) subcomplex after solubilization of membranes with n-dodecyl-beta-D-maltoside and subsequent nickel-nitrilotriacetic acid affinity chromatography. After co-reconstitution of the ab(2) subcomplex with purified subunit c, passive proton translocation rates as well as coupled ATPase activities after binding of F-1 were measured that were comparable with those of wild type F-0. The interaction between subunits a and b, which has been shown to be stoichiometric and functional, is not triggered by any cross-linking reagent and therefore reflects subunit interactions occurring within the F-0 complex in vivo.
ISSN: 00219258
DOI: 10.1074/jbc.M302027200

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