ArticleThe Journal of biological chemistry2015
Organization of Subunits in the Membrane Domain of the Bovine F-ATPase Revealed by Covalent Cross-linking.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 42 citations in OpenAlex.
- LyP vs advanced-stage CTCLs: single-cell profiling reveals markers of self-limited vs aggressive disease behavior.Blood advances · 2026Article
- Deciphering the enigma of RNA editing in the ATP1_alpha subunit of ATP synthase inSaudi journal of biological sciences · 2023Article
- Characterizing Endogenous Protein Complexes with Biological Mass Spectrometry.Chemical reviews · 2022Review
- Characterization of a highly diverged mitochondrial ATP synthase FThe Journal of biological chemistry · 2022Article
- Sequence and structure comparison of ATP synthase F0 subunits 6 and 8 in notothenioid fish.PloS one · 2021Article
- The circ_0004463/miR-380-3p/FOXO1 axis modulates mitochondrial respiration and bladder cancer cell apoptosis.Cell cycle (Georgetown, Tex.) · 2020Article
- Structure of the dimeric ATP synthase from bovine mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Mitochondrial DNA Mutation Analysis in Breast Cancer: Shifting From Germline Heteroplasmy Toward Homoplasmy in Tumors.Frontiers in oncology · 2020Article
- OSCP subunit of mitochondrial ATP synthase: role in regulation of enzyme function and of its transition to a pore.British journal of pharmacology · 2019Review
- Conformational Differences between Functional Human Immunodeficiency Virus Envelope Glycoprotein Trimers and Stabilized Soluble Trimers.Journal of virology · 2019Article
- Mitochondrial F-ATP Synthase and Its Transition into an Energy-Dissipating Molecular Machine.Oxidative medicine and cellular longevity · 2019Review
- USMG5 Ashkenazi Jewish founder mutation impairs mitochondrial complex V dimerization and ATP synthesis.Human molecular genetics · 2018Article
- Actively transcribed and expressedPeerJ · 2018Article
- The Peripheral Stalk of Rotary ATPases.Frontiers in physiology · 2018Review
- Heat Failure Phenotypes Induced by Knockdown of DAPIT in Zebrafish: A New Insight into Mechanism of Dilated Cardiomyopathy.Scientific reports · 2017Article
- Regulation of the HCellular and molecular life sciences : CMLS · 2017Review
- Persistence of the mitochondrial permeability transition in the absence of subunit c of human ATP synthase.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Mitochondrial protein interactome elucidated by chemical cross-linking mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structure of the mitochondrial ATP synthase fromProceedings of the National Academy of Sciences of the United States of America · 2016Article
- Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology.Molecular cell · 2016Article
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Authors and funding
7 authors at 2 institutions in 1 country.
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Abstract
The F-ATPase in bovine mitochondria is a membrane-bound complex of about 30 subunits of 18 different kinds. Currently, ∼85% of its structure is known. The enzyme has a membrane extrinsic catalytic domain, and a membrane intrinsic domain where the turning of the enzyme's rotor is generated from the transmembrane proton-motive force. The domains are linked by central and peripheral stalks. The central stalk and a hydrophobic ring of c-subunits in the membrane domain constitute the enzyme's rotor. The external surface of the catalytic domain and membrane subunit a are linked by the peripheral stalk, holding them static relative to the rotor. The membrane domain contains six additional subunits named ATP8, e, f, g, DAPIT (diabetes-associated protein in insulin-sensitive tissues), and 6.8PL (6.8-kDa proteolipid), each with a single predicted transmembrane α-helix, but their orientation and topography are unknown. Mutations in ATP8 uncouple the enzyme and interfere with its assembly, but its roles and the roles of the other five subunits are largely unknown. We have reacted accessible amino groups in the enzyme with bifunctional cross-linking agents and identified the linked residues. Cross-links involving the supernumerary subunits, where the structures are not known, show that the C terminus of ATP8 extends ∼70 Å from the membrane into the peripheral stalk and that the N termini of the other supernumerary subunits are on the same side of the membrane, probably in the mitochondrial matrix. These experiments contribute significantly toward building up a complete structural picture of the F-ATPase.
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