Mutations in C12orf62, a Factor that Couples COX I Synthesis with Cytochrome c Oxidase Assembly, Cause Fatal Neonatal Lactic Acidosis
We investigated a family in which the index subject presented with severe congenital lactic acidosis and dysmorphic features associated with a cytochrome c oxidase (COX)-assembly defect and a specific decrease in the synthesis of COX I, the subunit that nucleates COX assembly. Using a combination of...
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| Published in | American journal of human genetics Vol. 90; no. 1; pp. 142 - 151 |
|---|---|
| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Cambridge, MA
Elsevier Inc
13.01.2012
Cell Press Elsevier |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0002-9297 1537-6605 1537-6605 |
| DOI | 10.1016/j.ajhg.2011.11.027 |
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| Abstract | We investigated a family in which the index subject presented with severe congenital lactic acidosis and dysmorphic features associated with a cytochrome c oxidase (COX)-assembly defect and a specific decrease in the synthesis of COX I, the subunit that nucleates COX assembly. Using a combination of microcell-mediated chromosome transfer, homozygosity mapping, and transcript profiling, we mapped the gene defect to chromosome 12 and identified a homozygous missense mutation (c.88G>A) in C12orf62. C12orf62 was not detectable by immunoblot analysis in subject fibroblasts, and retroviral expression of the wild-type C12orf62 cDNA rescued the biochemical phenotype. Furthermore, siRNA-mediated knockdown of C12orf 62 recapitulated the biochemical defect in control cells and exacerbated it in subject cells. C12orf62 is apparently restricted to the vertebrate lineage. It codes for a very small (6 kDa), uncharacterized, single-transmembrane protein that localizes to mitochondria and elutes in a complex of ∼110 kDa by gel filtration. COX I, II, and IV coimmunoprecipated with an epitope-tagged version of C12orf62, and 2D blue-native-polyacrylamide-gel-electrophoresis analysis of newly synthesized mitochondrial COX subunits in subject fibroblasts showed that COX assembly was impaired and that the nascent enzyme complex was unstable. We conclude that C12orf62 is required for coordination of the early steps of COX assembly with the synthesis of COX I. |
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| AbstractList | We investigated a family in which the index subject presented with severe congenital lactic acidosis and dysmorphic features associated with a cytochrome c oxidase (COX)-assembly defect and a specific decrease in the synthesis of COX I, the subunit that nucleates COX assembly. Using a combination of microcell-mediated chromosome transfer, homozygosity mapping, and transcript profiling, we mapped the gene defect to chromosome 12 and identified a homozygous missense mutation (c.88G>A) in C12orf62. C12orf62 was not detectable by immunoblot analysis in subject fibroblasts, and retroviral expression of the wild-type C12orf62 cDNA rescued the biochemical phenotype. Furthermore, siRNA-mediated knockdown of C12orf 62 recapitulated the biochemical defect in control cells and exacerbated it in subject cells. C12orf62 is apparently restricted to the vertebrate lineage. It codes for a very small (6 kDa), uncharacterized, single-transmembrane protein that localizes to mitochondria and elutes in a complex of ∼110 kDa by gel filtration. COX I, II, and IV coimmunoprecipated with an epitope-tagged version of C12orf62, and 2D blue-native-polyacrylamide-gel-electrophoresis analysis of newly synthesized mitochondrial COX subunits in subject fibroblasts showed that COX assembly was impaired and that the nascent enzyme complex was unstable. We conclude that C12orf62 is required for coordination of the early steps of COX assembly with the synthesis of COX I.We investigated a family in which the index subject presented with severe congenital lactic acidosis and dysmorphic features associated with a cytochrome c oxidase (COX)-assembly defect and a specific decrease in the synthesis of COX I, the subunit that nucleates COX assembly. Using a combination of microcell-mediated chromosome transfer, homozygosity mapping, and transcript profiling, we mapped the gene defect to chromosome 12 and identified a homozygous missense mutation (c.88G>A) in C12orf62. C12orf62 was not detectable by immunoblot analysis in subject fibroblasts, and retroviral expression of the wild-type C12orf62 cDNA rescued the biochemical phenotype. Furthermore, siRNA-mediated knockdown of C12orf 62 recapitulated the biochemical defect in control cells and exacerbated it in subject cells. C12orf62 is apparently restricted to the vertebrate lineage. It codes for a very small (6 kDa), uncharacterized, single-transmembrane protein that localizes to mitochondria and elutes in a complex of ∼110 kDa by gel filtration. COX I, II, and IV coimmunoprecipated with an epitope-tagged version of C12orf62, and 2D blue-native-polyacrylamide-gel-electrophoresis analysis of newly synthesized mitochondrial COX subunits in subject fibroblasts showed that COX assembly was impaired and that the nascent enzyme complex was unstable. We conclude that C12orf62 is required for coordination of the early steps of COX assembly with the synthesis of COX I. We investigated a family in which the index subject presented with severe congenital lactic acidosis and dysmorphic features associated with a cytochrome c oxidase (COX)-assembly defect and a specific decrease in the synthesis of COX I, the subunit that nucleates COX assembly. Using a combination of microcell-mediated chromosome transfer, homozygosity mapping, and transcript profiling, we mapped the gene defect to chromosome 12 and identified a homozygous missense mutation (c.88G>A) in C12orf62. C12orf62 was not detectable by immunoblot analysis in subject fibroblasts, and retroviral expression of the wild-type C12orf62 cDNA rescued the biochemical phenotype. Furthermore, siRNA-mediated knockdown of C12orf 62 recapitulated the biochemical defect in control cells and exacerbated it in subject cells. C12orf62 is apparently restricted to the vertebrate lineage. It codes for a very small (6 kDa), uncharacterized, single-transmembrane protein that localizes to mitochondria and elutes in a complex of similar to 110 kDa by gel filtration. COX I, II, and IV coimmunoprecipated with an epitope-tagged version of C12orf62, and 2D blue-native-polyacrylamide-gel-electrophoresis analysis of newly synthesized mitochondrial COX subunits in subject fibroblasts showed that COX assembly was impaired and that the nascent enzyme complex was unstable. We conclude that C12orf62 is required for coordination of the early steps of COX assembly with the synthesis of COX I. We investigated a family in which the index subject presented with severe congenital lactic acidosis and dysmorphic features associated with a cytochrome c oxidase (COX)-assembly defect and a specific decrease in the synthesis of COX I, the subunit that nucleates COX assembly. Using a combination of microcell-mediated chromosome transfer, homozygosity mapping, and transcript profiling, we mapped the gene defect to chromosome 12 and identified a homozygous missense mutation (c.88G>A) in C12orf62. C12orf62 was not detectable by immunoblot analysis in subject fibroblasts, and retroviral expression of the wild-type C12orf62 cDNA rescued the biochemical phenotype. Furthermore, siRNA-mediated knockdown of C12orf 62 recapitulated the biochemical defect in control cells and exacerbated it in subject cells. C12orf62 is apparently restricted to the vertebrate lineage. It codes for a very small (6 kDa), uncharacterized, single-transmembrane protein that localizes to mitochondria and elutes in a complex of ~110 kDa by gel filtration. COX I, II, and IV coimmunoprecipated with an epitope-tagged version of C12orf62, and 2D blue-native-polyacrylamide-gel-electrophoresis analysis of newly synthesized mitochondrial COX subunits in subject fibroblasts showed that COX assembly was impaired and that the nascent enzyme complex was unstable. We conclude that C12orf62 is required for coordination of the early steps of COX assembly with the synthesis of COX I. [PUBLICATION ABSTRACT] We investigated a family in which the index subject presented with severe congenital lactic acidosis and dysmorphic features associated with a cytochrome c oxidase (COX)-assembly defect and a specific decrease in the synthesis of COX I, the subunit that nucleates COX assembly. Using a combination of microcell-mediated chromosome transfer, homozygosity mapping, and transcript profiling, we mapped the gene defect to chromosome 12 and identified a homozygous missense mutation (c.88G>A) in C12orf62 . C12orf62 was not detectable by immunoblot analysis in subject fibroblasts, and retroviral expression of the wild-type C12orf62 cDNA rescued the biochemical phenotype. Furthermore, siRNA-mediated knockdown of C12orf 62 recapitulated the biochemical defect in control cells and exacerbated it in subject cells. C12orf62 is apparently restricted to the vertebrate lineage. It codes for a very small (6 kDa), uncharacterized, single-transmembrane protein that localizes to mitochondria and elutes in a complex of ∼110 kDa by gel filtration. COX I, II, and IV coimmunoprecipated with an epitope-tagged version of C12orf62 , and 2D blue-native-polyacrylamide-gel-electrophoresis analysis of newly synthesized mitochondrial COX subunits in subject fibroblasts showed that COX assembly was impaired and that the nascent enzyme complex was unstable. We conclude that C12orf62 is required for coordination of the early steps of COX assembly with the synthesis of COX I. We investigated a family in which the index subject presented with severe congenital lactic acidosis and dysmorphic features associated with a cytochrome c oxidase (COX)-assembly defect and a specific decrease in the synthesis of COX I, the subunit that nucleates COX assembly. Using a combination of microcell-mediated chromosome transfer, homozygosity mapping, and transcript profiling, we mapped the gene defect to chromosome 12 and identified a homozygous missense mutation (c.88G>A) in C12orf62. C12orf62 was not detectable by immunoblot analysis in subject fibroblasts, and retroviral expression of the wild-type C12orf62 cDNA rescued the biochemical phenotype. Furthermore, siRNA-mediated knockdown of C12orf 62 recapitulated the biochemical defect in control cells and exacerbated it in subject cells. C12orf62 is apparently restricted to the vertebrate lineage. It codes for a very small (6 kDa), uncharacterized, single-transmembrane protein that localizes to mitochondria and elutes in a complex of ∼110 kDa by gel filtration. COX I, II, and IV coimmunoprecipated with an epitope-tagged version of C12orf62, and 2D blue-native-polyacrylamide-gel-electrophoresis analysis of newly synthesized mitochondrial COX subunits in subject fibroblasts showed that COX assembly was impaired and that the nascent enzyme complex was unstable. We conclude that C12orf62 is required for coordination of the early steps of COX assembly with the synthesis of COX I. We investigated a family in which the index subject presented with severe congenital lactic acidosis and dysmorphic features associated with a cytochrome c oxidase (COX)-assembly defect and a specific decrease in the synthesis of COX I, the subunit that nucleates COX assembly. Using a combination of microcell-mediated chromosome transfer, homozygosity mapping, and transcript profiling, we mapped the gene defect to chromosome 12 and identified a homozygous missense mutation (c.88G>A) in C12orf62. C12orf62 was not detectable by immunoblot analysis in subject fibroblasts, and retroviral expression of the wild-type C12orf62 cDNA rescued the biochemical phenotype. Furthermore, siRNA-mediated knockdown of C12orf 62 recapitulated the biochemical defect in control cells and exacerbated it in subject cells. C12orf62 is apparently restricted to the vertebrate lineage. It codes for a very small (6 kDa), uncharacterized, single-transmembrane protein that localizes to mitochondria and elutes in a complex of ∼110 kDa by gel filtration. COX I, II, and IV coimmunoprecipated with an epitope-tagged version of C12orf62, and 2D blue-native-polyacrylamide-gel-electrophoresis analysis of newly synthesized mitochondrial COX subunits in subject fibroblasts showed that COX assembly was impaired and that the nascent enzyme complex was unstable. We conclude that C12orf62 is required for coordination of the early steps of COX assembly with the synthesis of COX I. |
| Author | Antonicka, Hana Auré, Karine Nishimura, Tamiko Shoubridge, Eric A. Sasarman, Florin Weraarpachai, Woranontee Lombès, Anne Rötig, Agnès |
| AuthorAffiliation | 4 Institut Cochin, affiliated with the Institut National de la Santé et de la Recherche Médicale (Inserm; UMR-S 1016), the Centre National de la Recherche Scientifique (UMR 8104), and the Université Paris Descartes, Paris F-75014, France 1 Department of Human Genetics and Montreal Neurological Institute, McGill University, Montreal H3A 2B4, Quebec, Canada 2 Hôpital Ambroise Paré, Assistance Publique-Hôpitaux de Paris (AP-HP), Boulogne-Billancourt, Paris F-92100, France 3 Unité de Formation et de Recherche, la Faculté de Médecine Paris Île-de-France Ouest, Paris F-78280, France 5 Université Paris Descartes and Inserm U781, 149 rue de Sèvres, Paris 75015, France 6 Unité de Cardiogénétique et Myogénétique Moléculaire et Cellulaire, Service de Biochimie Métabolique, Groupe Hospitalier Pitié-Salpêtrière (Paris), AP-HP, Paris F-75651, France |
| AuthorAffiliation_xml | – name: 6 Unité de Cardiogénétique et Myogénétique Moléculaire et Cellulaire, Service de Biochimie Métabolique, Groupe Hospitalier Pitié-Salpêtrière (Paris), AP-HP, Paris F-75651, France – name: 3 Unité de Formation et de Recherche, la Faculté de Médecine Paris Île-de-France Ouest, Paris F-78280, France – name: 1 Department of Human Genetics and Montreal Neurological Institute, McGill University, Montreal H3A 2B4, Quebec, Canada – name: 4 Institut Cochin, affiliated with the Institut National de la Santé et de la Recherche Médicale (Inserm; UMR-S 1016), the Centre National de la Recherche Scientifique (UMR 8104), and the Université Paris Descartes, Paris F-75014, France – name: 5 Université Paris Descartes and Inserm U781, 149 rue de Sèvres, Paris 75015, France – name: 2 Hôpital Ambroise Paré, Assistance Publique-Hôpitaux de Paris (AP-HP), Boulogne-Billancourt, Paris F-92100, France |
| Author_xml | – sequence: 1 givenname: Woranontee surname: Weraarpachai fullname: Weraarpachai, Woranontee organization: Department of Human Genetics and Montreal Neurological Institute, McGill University, Montreal H3A 2B4, Quebec, Canada – sequence: 2 givenname: Florin surname: Sasarman fullname: Sasarman, Florin organization: Department of Human Genetics and Montreal Neurological Institute, McGill University, Montreal H3A 2B4, Quebec, Canada – sequence: 3 givenname: Tamiko surname: Nishimura fullname: Nishimura, Tamiko organization: Department of Human Genetics and Montreal Neurological Institute, McGill University, Montreal H3A 2B4, Quebec, Canada – sequence: 4 givenname: Hana surname: Antonicka fullname: Antonicka, Hana organization: Department of Human Genetics and Montreal Neurological Institute, McGill University, Montreal H3A 2B4, Quebec, Canada – sequence: 5 givenname: Karine surname: Auré fullname: Auré, Karine organization: Hôpital Ambroise Paré, Assistance Publique-Hôpitaux de Paris (AP-HP), Boulogne-Billancourt, Paris F-92100, France – sequence: 6 givenname: Agnès surname: Rötig fullname: Rötig, Agnès organization: Université Paris Descartes and Inserm U781, 149 rue de Sèvres, Paris 75015, France – sequence: 7 givenname: Anne surname: Lombès fullname: Lombès, Anne organization: Institut Cochin, affiliated with the Institut National de la Santé et de la Recherche Médicale (Inserm; UMR-S 1016), the Centre National de la Recherche Scientifique (UMR 8104), and the Université Paris Descartes, Paris F-75014, France – sequence: 8 givenname: Eric A. surname: Shoubridge fullname: Shoubridge, Eric A. email: eric@ericpc.mni.mcgill.ca organization: Department of Human Genetics and Montreal Neurological Institute, McGill University, Montreal H3A 2B4, Quebec, Canada |
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| Copyright | 2012 The American Society of Human Genetics 2015 INIST-CNRS Copyright © 2012 The American Society of Human Genetics. Published by Elsevier Inc. All rights reserved. Copyright Cell Press Jan 13, 2012 2012 The American Society of Human Genetics. Published by Elsevier Ltd. All right reserved. 2012 The American Society of Human Genetics |
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| Keywords | Human Neonatal Enzyme Couple Cytochrome-c oxidase Fatal course Newborn Synthesis Genetics Oxidoreductases Lactic acid Mutation Metabolic acidosis |
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| Snippet | We investigated a family in which the index subject presented with severe congenital lactic acidosis and dysmorphic features associated with a cytochrome c... We investigated a family in which the index subject presented with severe congenital lactic acidosis and dysmorphic features associated with a cytochrome c... |
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| SubjectTerms | Acidosis, Lactic - genetics Biological and medical sciences Chromosomes Cyclooxygenase 1 - biosynthesis Electron Transport Complex IV - biosynthesis Fatal Outcome Female Fibroblasts - enzymology Fundamental and applied biological sciences. Psychology Gene expression General aspects. Genetic counseling Genetic research Genetics of eukaryotes. Biological and molecular evolution Homozygote Humans Infant, Newborn Medical genetics Medical sciences Membrane Proteins - genetics Membranes Mitochondria - enzymology Mitochondria - genetics Mitochondrial Proteins - genetics Molecular and cellular biology Mutation Mutation, Missense Protein synthesis |
| Title | Mutations in C12orf62, a Factor that Couples COX I Synthesis with Cytochrome c Oxidase Assembly, Cause Fatal Neonatal Lactic Acidosis |
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