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Mitochondrion. 2017 Nov;37:55-61. doi: 10.1016/j.mito.2017.07.001. Epub 2017 Jul 8.

LYRM7 - associated complex III deficiency: A clinical, molecular genetic, MR tomographic, and biochemical study.

Author information

1
Institute of Human Genetics, University Medical Center Hamburg-Eppendorf, Hamburg, Germany. Electronic address: m.hempel@uke.de.
2
Institute of Human Genetics, Helmholtz Center Munich, Munich, Germany.
3
Department of Pediatrics, University Medical Center Hamburg-Eppendorf, Hamburg, Germany.
4
Institute of Human Genetics, Technical University Munich, Munich, Germany.
5
Institute of Human Genetics, Helmholtz Center Munich, Munich, Germany; Institute of Human Genetics, Technical University Munich, Munich, Germany.
6
Department of Diagnostic and Interventional Neuroradiology, University Medical Center Hamburg-Eppendorf, Hamburg, Germany.
7
Department of Pediatrics, Paracelsus Medical University Salzburg, Salzburg, Austria.

Abstract

LYRM7 is involved in the last steps of mitochondrial complex III assembly where it acts as a chaperone for the Rieske iron‑sulfur (Fe-S) protein in the mitochondrial matrix. Using exome sequencing, we identified homozygosity for a splice site destroying 4 base pair deletion in LYRM7 in a child with recurrent lactic acidotic crises and distinct early-onset leukencephalopathy. Sanger sequencing showed variant segregation in similarly affected family members. Functional analyses revealed a reduced amount of the Rieske Fe-S protein, which was restored after re-expression of LYRM7. Our data provide further evidence for the importance of LYRM7 for mitochondrial function and emphasize the importance of whole exome sequencing in the diagnosis of rare mitochondrial diseases.

KEYWORDS:

Complex III; Encephalopathy; LYRM7; Lactic acidosis; Mitochondriopathy; Whole exome sequencing

PMID:
28694194
DOI:
10.1016/j.mito.2017.07.001
[Indexed for MEDLINE]

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