Exome Sequence Reveals Mutations in CoA Synthase as a Cause of Neurodegeneration with Brain Iron Accumulation
Neurodegeneration with brain iron accumulation (NBIA) comprises a clinically and genetically heterogeneous group of disorders with progressive extrapyramidal signs and neurological deterioration, characterized by iron accumulation in the basal ganglia. Exome sequencing revealed the presence of reces...
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| Published in | American journal of human genetics Vol. 94; no. 1; pp. 11 - 22 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
02.01.2014
Cell Press Elsevier |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Neurodegeneration with brain iron accumulation (NBIA) comprises a clinically and genetically heterogeneous group of disorders with progressive extrapyramidal signs and neurological deterioration, characterized by iron accumulation in the basal ganglia. Exome sequencing revealed the presence of recessive missense mutations in COASY, encoding coenzyme A (CoA) synthase in one NBIA-affected subject. A second unrelated individual carrying mutations in COASY was identified by Sanger sequence analysis. CoA synthase is a bifunctional enzyme catalyzing the final steps of CoA biosynthesis by coupling phosphopantetheine with ATP to form dephospho-CoA and its subsequent phosphorylation to generate CoA. We demonstrate alterations in RNA and protein expression levels of CoA synthase, as well as CoA amount, in fibroblasts derived from the two clinical cases and in yeast. This is the second inborn error of coenzyme A biosynthesis to be implicated in NBIA. |
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| AbstractList | Neurodegeneration with brain iron accumulation (NBIA) comprises a clinically and genetically heterogeneous group of disorders with progressive extrapyramidal signs and neurological deterioration, characterized by iron accumulation in the basal ganglia. Exome sequencing revealed the presence of recessive missense mutations in COASY, encoding coenzyme A (CoA) synthase in one NBIA-affected subject. A second unrelated individual carrying mutations in COASY was identified by Sanger sequence analysis. CoA synthase is a bifunctional enzyme catalyzing the final steps of CoA biosynthesis by coupling phosphopantetheine with ATP to form dephospho-CoA and its subsequent phosphorylation to generate CoA. We demonstrate alterations in RNA and protein expression levels of CoA synthase, as well as CoA amount, in fibroblasts derived from the two clinical cases and in yeast. This is the second inborn error of coenzyme A biosynthesis to be implicated in NBIA. [PUBLICATION ABSTRACT] Neurodegeneration with brain iron accumulation (NBIA) comprises a clinically and genetically heterogeneous group of disorders with progressive extrapyramidal signs and neurological deterioration, characterized by iron accumulation in the basal ganglia. Exome sequencing revealed the presence of recessive missense mutations in COASY, encoding coenzyme A (CoA) synthase in one NBIA-affected subject. A second unrelated individual carrying mutations in COASY was identified by Sanger sequence analysis. CoA synthase is a bifunctional enzyme catalyzing the final steps of CoA biosynthesis by coupling phosphopantetheine with ATP to form dephospho-CoA and its subsequent phosphorylation to generate CoA. We demonstrate alterations in RNA and protein expression levels of CoA synthase, as well as CoA amount, in fibroblasts derived from the two clinical cases and in yeast. This is the second inborn error of coenzyme A biosynthesis to be implicated in NBIA. Neurodegeneration with brain iron accumulation (NBIA) comprises a clinically and genetically heterogeneous group of disorders with progressive extrapyramidal signs and neurological deterioration, characterized by iron accumulation in the basal ganglia. Exome sequencing revealed the presence of recessive missense mutations in COASY, encoding coenzyme A (CoA) synthase in one NBIA-affected subject. A second unrelated individual carrying mutations in COASY was identified by Sanger sequence analysis. CoA synthase is a bifunctional enzyme catalyzing the final steps of CoA biosynthesis by coupling phosphopantetheine with ATP to form dephospho-CoA and its subsequent phosphorylation to generate CoA. We demonstrate alterations in RNA and protein expression levels of CoA synthase, as well as CoA amount, in fibroblasts derived from the two clinical cases and in yeast. This is the second inborn error of coenzyme A biosynthesis to be implicated in NBIA.Neurodegeneration with brain iron accumulation (NBIA) comprises a clinically and genetically heterogeneous group of disorders with progressive extrapyramidal signs and neurological deterioration, characterized by iron accumulation in the basal ganglia. Exome sequencing revealed the presence of recessive missense mutations in COASY, encoding coenzyme A (CoA) synthase in one NBIA-affected subject. A second unrelated individual carrying mutations in COASY was identified by Sanger sequence analysis. CoA synthase is a bifunctional enzyme catalyzing the final steps of CoA biosynthesis by coupling phosphopantetheine with ATP to form dephospho-CoA and its subsequent phosphorylation to generate CoA. We demonstrate alterations in RNA and protein expression levels of CoA synthase, as well as CoA amount, in fibroblasts derived from the two clinical cases and in yeast. This is the second inborn error of coenzyme A biosynthesis to be implicated in NBIA. Neurodegeneration with brain iron accumulation (NBIA) comprises a clinically and genetically heterogeneous group of disorders with progressive extrapyramidal signs and neurological deterioration, characterized by iron accumulation in the basal ganglia. Exome sequencing revealed the presence of recessive missense mutations in COASY, encoding coenzyme A (CoA) synthase in one NBIA-affected subject. A second unrelated individual carrying mutations in COASY was identified by Sanger sequence analysis. CoA synthase is a bifunctional enzyme catalyzing the final steps of CoA biosynthesis by coupling phosphopantetheine with ATP to form dephospho-CoA and its subsequent phosphorylation to generate CoA. We demonstrate alterations in RNA and protein expression levels of CoA synthase, as well as CoA amount, in fibroblasts derived from the two clinical cases and in yeast. This is the second inborn error of coenzyme A biosynthesis to be implicated in NBIA. |
| Author | Invernizzi, Federica Schwarzmayr, Thomas Dusi, Sabrina Gregory, Allison Tiranti, Valeria Hamada, Jeffrey Tigano, Marco Gout, Ivan Tsuchiya, Yugo Pasqualato, Sebastiano Strom, Tim M. Garavaglia, Barbara Nardocci, Nardo Hayflick, Susan Venco, Paola Demchenko, Nikita Kurian, Manju A. Wieland, Thomas Bettencourt, Conceição Zorzi, Giovanna Sanford, Lynn Valletta, Lorella Houlden, Henry Goffrini, Paola Haack, Tobias B. Chiapparini, Luisa Prokisch, Holger |
| AuthorAffiliation | 11 Neurosciences Unit, UCL-Institute of Child Health, Great Ormond Street Hospital, London WC1N 3JH, UK 7 Department of Molecular & Medical Genetics, Oregon Health & Science University, Portland, OR 97329, USA 5 Crystallography Unit, Department of Experimental Oncology, European Institute of Oncology, IFOM-IEO Campus, 20139 Milan, Italy 6 Department of Life Sciences, University of Parma, 43124 Parma, Italy 1 Unit of Molecular Neurogenetics – Pierfranco and Luisa Mariani Center for the study of Mitochondrial Disorders in Children, IRCCS Foundation Neurological Institute “C. Besta,” 20126 Milan, Italy 9 Unit of Neuroradiology, IRCCS Foundation Neurological Institute “C. Besta,” 20133 Milan, Italy 4 Institute of Structural and Molecular Biology, University College London, London WC1E 6BT, UK 8 UCL Institute of Neurology and The National Hospital for Neurology and Neurosurgery, Queen Square, London WC1N 3BG, UK 3 Institute of Human Genetics, Helmholtz Zentrum München, 85764 Munich, Germany 12 Depar |
| AuthorAffiliation_xml | – name: 12 Department of Neurology, Great Ormond Street Hospital, London WC1N 3JH, UK – name: 1 Unit of Molecular Neurogenetics – Pierfranco and Luisa Mariani Center for the study of Mitochondrial Disorders in Children, IRCCS Foundation Neurological Institute “C. Besta,” 20126 Milan, Italy – name: 6 Department of Life Sciences, University of Parma, 43124 Parma, Italy – name: 11 Neurosciences Unit, UCL-Institute of Child Health, Great Ormond Street Hospital, London WC1N 3JH, UK – name: 9 Unit of Neuroradiology, IRCCS Foundation Neurological Institute “C. Besta,” 20133 Milan, Italy – name: 10 Unit of Child Neurology, IRCCS Foundation Neurological Institute “C. Besta,” 20133 Milan, Italy – name: 8 UCL Institute of Neurology and The National Hospital for Neurology and Neurosurgery, Queen Square, London WC1N 3BG, UK – name: 2 Institute of Human Genetics, Technische Universität München, 81675 Munich, Germany – name: 3 Institute of Human Genetics, Helmholtz Zentrum München, 85764 Munich, Germany – name: 5 Crystallography Unit, Department of Experimental Oncology, European Institute of Oncology, IFOM-IEO Campus, 20139 Milan, Italy – name: 7 Department of Molecular & Medical Genetics, Oregon Health & Science University, Portland, OR 97329, USA – name: 4 Institute of Structural and Molecular Biology, University College London, London WC1E 6BT, UK |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/24360804$$D View this record in MEDLINE/PubMed |
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| Copyright | 2014 The American Society of Human Genetics Copyright © 2014 The American Society of Human Genetics. Published by Elsevier Inc. All rights reserved. Copyright Cell Press Jan 2, 2014 2014 The American Society of Human Genetics. Published by Elsevier Ltd. All right reserved. 2014 The American Society of Human Genetics |
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| Title | Exome Sequence Reveals Mutations in CoA Synthase as a Cause of Neurodegeneration with Brain Iron Accumulation |
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