COA6 is structurally tuned to function as a thiol-disulfide oxidoreductase in copper delivery to mitochondrial cytochrome c oxidase

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dc.citation.titleCell Reportses
dc.citation.volume29(12)es
dc.creatorSoma, Shivatheja
dc.creatorMorgada, Marcos Nicolás
dc.creatorNaik, Mandar T.
dc.creatorBoulet, Aren
dc.creatorRoesler, Anna A.
dc.creatorDziuba, Nathaniel
dc.creatorGhosh, Alok
dc.creatorYu, Qinhong
dc.creatorLindahl, Paul A.
dc.creatorAmes, James B.
dc.creatorLeary, Scot C.
dc.creatorVila, Alejandro J.
dc.creatorGohil, Vishal M.
dc.date.accessioned2021-03-03T17:21:28Z
dc.date.available2021-03-03T17:21:28Z
dc.date.issued2019-12-17
dc.descriptionIn eukaryotes, cellular respiration is driven by mitochondrial cytochrome c oxidase (CcO), an enzyme complex that requires copper cofactors for its catalytic activity. Insertion of copper into its catalytically active subunits, including COX2, is a complex process that requires metallochaperones and redox proteins including SCO1, SCO2, and COA6, a recently discovered protein whose molecular function is unknown. To uncover the molecular mechanism by which COA6 and SCO proteins mediate copper delivery to COX2, we have solved the solution structure of COA6, which reveals a coiled-coil-helix-coiled-coilhelix domain typical of redox-active proteins found in the mitochondrial inter-membrane space. Accordingly, we demonstrate that COA6 can reduce the copper-coordinating disulfides of its client proteins, SCO1 and COX2, allowing for copper binding. Finally, our determination of the interaction surfaces and reduction potentials of COA6 and its client proteins provides a mechanism of how metallochaperone and disulfide reductase activities are coordinated to deliver copper to CcO.es
dc.description.filFil: Soma, Shivatheja. Texas A&M University. Department of Biochemistry and Biophysics; United States.es
dc.description.filFil: Morgada, Marcos N. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR -CONICET); Argentina.es
dc.description.filFil: Morgada, Marcos N. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química Biológica. Área Biofísica; Argentina.es
dc.description.filFil: Naik, Mandar T. Texas A&M University. Department of Biochemistry and Biophysics; United States.es
dc.description.filFil: Naik, Mandar T. Brown University. Department of Molecular Pharmacology, Physiology, and Biotechnology; United States.es
dc.description.filFil: Boulet, Aren. University of Saskatchewan. Department of Biochemistry, Microbiology and Immunology; Canada.es
dc.description.filFil: Roesler, Anna A. University of Saskatchewan. Department of Biochemistry, Microbiology and Immunology; Canada.es
dc.description.filFil: Dziuba, Nathaniel. Texas A&M University. Department of Biochemistry and Biophysics; United States.es
dc.description.filFil: Ghosh, Alok. Texas A&M University. Department of Biochemistry and Biophysics; United States.es
dc.description.filFil: Ghosh, Alok. University of Calcutta. Department of Biochemistry; India.es
dc.description.filFil: Yu, Qinhong. University of California. Department of Chemistry; United States.es
dc.description.filFil: Lindahl, Paul A. Texas A&M University. Department of Biochemistry and Biophysics; United States.es
dc.description.filFil: Lindahl, Paul A. Texas A&M University. Department of Chemistry; United States.es
dc.description.filFil: Ames, James B. University of California. Department of Chemistry; United States.es
dc.description.filFil: Leary, Scot C. University of Saskatchewan. Department of Biochemistry, Microbiology and Immunology; Canada.es
dc.description.filFil: Vila, Alejandro J. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR -CONICET); Argentina.es
dc.description.filFil: Vila, Alejandro J. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química Biológica. Área Biofísica; Argentina.es
dc.description.filFil: Gohil, Vishal M. Texas A&M University. Department of Biochemistry and Biophysics; United States.es
dc.description.sponsorshipNational Institutes of Health (NIH): awards R01GM111672, R35GM127021 and R01EY012347es
dc.description.sponsorshipWelch Foundation: grant A-1810es
dc.description.sponsorshipTexas A&M University: T3 grantes
dc.description.sponsorshipCanadian Institutes of Health Research Operating: grant MOP 133562es
dc.formatapplication/pdf
dc.format.extent4114–4126es
dc.identifier.issn2211-1247es
dc.identifier.urihttp://hdl.handle.net/2133/19986
dc.language.isoenges
dc.publisherCell Presses
dc.relation.publisherversionhttps://doi.org/10.1016/j.celrep.2019.11.054es
dc.relation.publisherversionhttps://www.cell.com/cell-reports/fulltext/S2211-1247(19)31536-0?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS2211124719315360%3Fshowall%3Dtruees
dc.rightsopenAccesses
dc.rights.holderUniversidad Nacional de Rosarioes
dc.rights.holderSoma, Shivathejaes
dc.rights.holderMorgada, Marcos N.es
dc.rights.holderNaik, Mandar T.es
dc.rights.holderBoulet, Arenes
dc.rights.holderRoesler, Anna A.es
dc.rights.holderDziuba, Nathanieles
dc.rights.holderGhosh, Alokes
dc.rights.holderYu, Qinhonges
dc.rights.holderLindahl, Paul A.es
dc.rights.holderAmes, James B.es
dc.rights.holderLeary, Scot C.es
dc.rights.holderVila, Alejandro J.es
dc.rights.holderGohil, Vishal M.es
dc.rights.textAttribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)es
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectCytochrome c Oxidase Assembly factor 6 (COA6)es
dc.subjectCytochrome c Oxidase subunit 2 (COX2)es
dc.subjectMitochondriaes
dc.subjectSCO1 Cytochrome c Oxidase Assembly Protein 1es
dc.subjectSCO2 Cytochrome c Oxidase Assembly Protein 2es
dc.subjectCopperes
dc.subjectMetallochaperoneses
dc.titleCOA6 is structurally tuned to function as a thiol-disulfide oxidoreductase in copper delivery to mitochondrial cytochrome c oxidasees
dc.typearticle
dc.typeartículo
dc.typepublishedVersion
dc.type.collectionarticulo
dc.type.versionpublishedVersiones

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