ArticleFEBS letters2013
Interactions between subunits a and b in the rotary ATP synthase as determined by cross-linking.
Article in FEBS letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Engineered Cross-Linking to Study the Pore Architecture of the CRAC Channel.Methods in molecular biology (Clifton, N.J.) · 2018Article
- The Peripheral Stalk of Rotary ATPases.Frontiers in physiology · 2018Review
- Analysis of an N-terminal deletion in subunit a of the Escherichia coli ATP synthase.Journal of bioenergetics and biomembranes · 2017Article
- Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology.Molecular cell · 2016Article
- Article
- Mitochondrial DNA Sequence and Lack of Response to Anoxia in the Annual Killifish Austrofundulus limnaeus.Frontiers in physiology · 2016Article
- Fo-driven Rotation in the ATP Synthase Direction against the Force of F1 ATPase in the FoF1 ATP Synthase.The Journal of biological chemistry · 2015Article
- Understanding structure, function, and mutations in the mitochondrial ATP synthase.Microbial cell (Graz, Austria) · 2015Article
- Interacting cytoplasmic loops of subunits a and c of Escherichia coli F1F0 ATP synthase gate H+ transport to the cytoplasm.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- High-resolution structure and mechanism of an F/V-hybrid rotor ring in a Na⁺-coupled ATP synthase.Nature communications · 2014Article
- Article
- Escherichia coli F1Fo-ATP synthase with a b/δ fusion protein allows analysis of the function of the individual b subunits.The Journal of biological chemistry · 2013Article
- Individual interactions of the b subunits within the stator of the Escherichia coli ATP synthase.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
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 connecting TM4 and TM5 of subunit a. Finally, benzophenone-4-maleimide derivatized Cys in the 2-3 periplasmic loop of subunit a were shown to cross-link with the periplasmic N-terminal region of subunit b. These experiments help to define the juxtaposition of subunits b and a in the ATP synthase.
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Registered trials
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