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dc.contributor.authorWalpole, T. B.en
dc.contributor.authorPalmer, David N.en
dc.contributor.authorJiang, Huibingen
dc.contributor.authorDing, S.en
dc.contributor.authorFearnley, I. M.en
dc.contributor.authorWalker, J. E.en
dc.date.accessioned2017-12-18T00:38:05Z
dc.date.available2015-01-21en
dc.date.issued2015-04-01en
dc.identifier.citationWalpole et al. (2015). Conservation of complete trimethylation of lysine-43 in the rotor ring of c-subunits of metazoan adenosine triphosphate (ATP) synthases. Molecular and Cellular Proteomics, 14(4), 828-840. doi:10.1074/mcp.M114.047456en
dc.identifier.issn1535-9476en
dc.identifier.urihttps://hdl.handle.net/10182/8852
dc.description.abstractThe rotors of ATP synthases turn about 100 times every second. One essential component of the rotor is a ring of hydrophobic c-subunits in the membrane domain of the enzyme. The rotation of these c-rings is driven by a transmembrane proton-motive force, and they turn against a surface provided by another membrane protein, known as subunit a. Together, the rotating c-ring and the static subunit a provide a pathway for protons through the membrane in which the c-ring and subunit a are embedded. Vertebrate and invertebrate c-subunits are well conserved. In the structure of the bovine F₁-ATPase-c-ring subcomplex, the 75 amino acid c-subunit is folded into two transmembrane α-helices linked by a short loop. Each bovine rotor-ring consists of eight c-subunits with the N- and C-terminal α-helices forming concentric inner and outer rings, with the loop regions exposed to the phospholipid head-group region on the matrix side of the inner membrane. Lysine-43 is in the loop region and its ε-amino group is completely trimethylated. The role of this modification is unknown. If the trimethylated lysine-43 plays some important role in the functioning, assembly or degradation of the c-ring, it would be expected to persist throughout vertebrates and possibly invertebrates also. Therefore, we have carried out a proteomic analysis of c-subunits across representative species from different classes of vertebrates and from invertebrate phyla. In the twenty-nine metazoan species that have been examined, the complete methylation of lysine-43 is conserved, and it is likely to be conserved throughout the more than two million extant metazoan species. In unicellular eukaryotes and prokaryotes, when the lysine is conserved it is unmethylated, and the stoichiometries of c-subunits vary from 9-15. One possible role for the trimethylated residue is to provide a site for the specific binding of cardiolipin, an essential component of ATP synthases in mitochondria.en
dc.format.extent828-840en
dc.language.isoenen
dc.publisherAmerican Society for Biochemistry and Molecular Biologyen
dc.relationThe original publication is available from - American Society for Biochemistry and Molecular Biology - https://doi.org/10.1074/mcp.M114.047456en
dc.relation.urihttps://doi.org/10.1074/mcp.M114.047456en
dc.rights© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.en
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectATP synthaseen
dc.subjectc-subunitsen
dc.subjectrotoren
dc.subjectmitochondriaen
dc.subjectBiochemistry & Molecular Biologyen
dc.subject.meshAnimalsen
dc.subject.meshHumansen
dc.subject.meshInvertebratesen
dc.subject.meshProton-Translocating ATPasesen
dc.subject.meshLysineen
dc.subject.meshPeptidesen
dc.subject.meshProtein Subunitsen
dc.subject.meshSpectrometry, Mass, Electrospray Ionizationen
dc.subject.meshPhylogenyen
dc.subject.meshProtein Processing, Post-Translationalen
dc.subject.meshAmino Acid Sequenceen
dc.subject.meshConserved Sequenceen
dc.subject.meshMethylationen
dc.subject.meshMolecular Weighten
dc.subject.meshMolecular Sequence Dataen
dc.subject.meshTandem Mass Spectrometryen
dc.titleConservation of complete trimethylation of lysine-43 in the rotor ring of c-subunits of metazoan adenosine triphosphate (ATP) synthasesen
dc.typeJournal Article
lu.contributor.unitLincoln Universityen
lu.contributor.unitFaculty of Agriculture and Life Sciencesen
lu.contributor.unitDepartment of Wine, Food and Molecular Biosciencesen
lu.contributor.unitResearch Management Officeen
lu.contributor.unit/LU/Research Management Office/2018 PBRF Staff groupen
dc.identifier.doi10.1074/mcp.M114.047456en
dc.subject.anzsrc060109 Proteomics and Intermolecular Interactions (Excl. Medical Proteomics)en
dc.subject.anzsrc060107 Enzymesen
dc.subject.anzsrc0601 Biochemistry and Cell Biologyen
dc.subject.anzsrcMD Multidisciplinaryen
dc.relation.isPartOfMolecular and Cellular Proteomicsen
pubs.issue4en
pubs.organisational-group/LU
pubs.organisational-group/LU/Agriculture and Life Sciences
pubs.organisational-group/LU/Agriculture and Life Sciences/WFMB
pubs.organisational-group/LU/Research Management Office
pubs.organisational-group/LU/Research Management Office/2018 PBRF Staff group
pubs.publication-statusPublisheden
pubs.volume14en
dc.identifier.eissn1535-9484en
dc.rights.licenceAttributionen
lu.identifier.orcid0000-0002-9703-5351


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