Interactions between subunits a and b in the rotary ATP synthase as determined by cross-linking.

Journal article

The interaction of the membrane traversing stator subunits a and b of the rotary ATP synthase was probed by substitution of a single Cys into each subunit with subsequent Cu(2+) catalyzed cross-linking. Extensive interaction between the transmembrane (TM) region of one b subunit and TM2 of subunit a was indicated by cross-linking with 6 Cys pairs introduced into these regions. Additional disulfide cross-linking was observed between the N-terminus of subunit b and the periplasmic loop connecti...

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Authors: DeLeon-Rangel, J; Ishmukhametov, R; Jiang, W; Fillingame, R; Vik, S

• Journal: FEBS letters
• Volume: 587
• Issue: 7
• Pages: 892-897
• Publication date: 2013-04-01
• DOI: 10.1016/j.febslet.2013.02.012
• EISSN: 1873-3468
• ISSN: 0014-5793
• Language: English
• Keywords: Escherichia coli Proteins; Binding Sites; Escherichia coli; Cysteine; ATP Synthetase Complexes; Protein Binding; Protein Structure, Tertiary; Benzophenones; Models, Molecular; Mutation; Bacterial Proton-Translocating ATPases; Maleimides; Disulfides; Cross-Linking Reagents; Protein Multimerization; Immunoblotting