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 |
Zur Langanzeige
Seitenaufrufe
2
Letzte Woche
0
0
Letzter Monat
0
0
geprüft am 10.05.2024