Homozygous missense mutation in UQCRC2 associated with severe encephalomyopathy, mitochondrial complex III assembly defect and activation of mitochondrial protein quality control.

Caseinolytic mitochondrial matrix peptidase proteolytic subunit (CLPP) Mitochondrial complex III Mitochondrial dysfunction Mitochondrial protein quality control Respiratory supercomplexes UQCRC2 (Core2, Core 2)

Journal

Biochimica et biophysica acta. Molecular basis of disease
ISSN: 1879-260X
Titre abrégé: Biochim Biophys Acta Mol Basis Dis
Pays: Netherlands
ID NLM: 101731730

Informations de publication

Date de publication:
01 08 2021
Historique:
received: 11 12 2020
revised: 31 03 2021
accepted: 12 04 2021
pubmed: 19 4 2021
medline: 18 11 2021
entrez: 18 4 2021
Statut: ppublish

Résumé

The mitochondrial respiratory chain (MRC) complex III (CIII) associates with complexes I and IV (CI and CIV) into supercomplexes. We identified a novel homozygous missense mutation (c.665G>C; p.Gly222Ala) in UQCRC2 coding for structural subunit Core 2 in a patient with severe encephalomyopathy. The structural data suggest that the Gly222Ala exchange might result in an altered spatial arrangement in part of the UQCRC2 subunit, which could impact specific protein-protein interactions. Accordingly, we have found decreased levels of CIII and accumulation of CIII-specific subassemblies comprising MT-CYB, UQCRB, UQCRQ, UQCR10 and CYC1 subunits, but devoid of UQCRC1, UQCRC2, and UQCRFS1 in the patient's fibroblasts. The lack of UQCRC1 subunit-containing subassemblies could result from an impaired interaction with mutant UQCRC2

Identifiants

pubmed: 33865955
pii: S0925-4439(21)00080-6
doi: 10.1016/j.bbadis.2021.166147
pii:
doi:

Substances chimiques

Mitochondrial Proteins 0
Electron Transport Complex III EC 7.1.1.8

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

166147

Informations de copyright

Copyright © 2021 Elsevier B.V. All rights reserved.

Auteurs

Daniela Burska (D)

Department of Paediatrics and Inherited Metabolic Disorders, First Faculty of Medicine, Charles University, General University Hospital, Prague, Czech Republic.

Lukas Stiburek (L)

Department of Paediatrics and Inherited Metabolic Disorders, First Faculty of Medicine, Charles University, General University Hospital, Prague, Czech Republic.

Jana Krizova (J)

Department of Paediatrics and Inherited Metabolic Disorders, First Faculty of Medicine, Charles University, General University Hospital, Prague, Czech Republic.

Marie Vanisova (M)

Department of Paediatrics and Inherited Metabolic Disorders, First Faculty of Medicine, Charles University, General University Hospital, Prague, Czech Republic.

Vaclav Martinek (V)

Department of Biochemistry, Faculty of Science, Charles University, Prague, Czech Republic.

Jana Sladkova (J)

Department of Paediatrics and Inherited Metabolic Disorders, First Faculty of Medicine, Charles University, General University Hospital, Prague, Czech Republic.

Josef Zamecnik (J)

Department of Pathology and Molecular Medicine, 2nd Faculty of Medicine, Charles University, Motol University Hospital, Prague, Czech Republic.

Tomas Honzik (T)

Department of Paediatrics and Inherited Metabolic Disorders, First Faculty of Medicine, Charles University, General University Hospital, Prague, Czech Republic.

Jiri Zeman (J)

Department of Paediatrics and Inherited Metabolic Disorders, First Faculty of Medicine, Charles University, General University Hospital, Prague, Czech Republic.

Hana Hansikova (H)

Department of Paediatrics and Inherited Metabolic Disorders, First Faculty of Medicine, Charles University, General University Hospital, Prague, Czech Republic.

Marketa Tesarova (M)

Department of Paediatrics and Inherited Metabolic Disorders, First Faculty of Medicine, Charles University, General University Hospital, Prague, Czech Republic. Electronic address: marketa.tesarova@lf1.cuni.cz.

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Classifications MeSH