LYRM7 - associated complex III deficiency: A clinical, molecular genetic, MR tomographic, and biochemical study
2017; Elsevier BV; Volume: 37; Linguagem: Inglês
10.1016/j.mito.2017.07.001
ISSN1872-8278
AutoresMaja Hempel, Laura S. Kremer, Konstantinos Tsiakas, Bader Alhaddad, Tobias B. Haack, Ulrike Löbel, René G. Feichtinger, Wolfgang Sperl, Holger Prokisch, Johannes A. Mayr, René Santer,
Tópico(s)RNA modifications and cancer
ResumoLYRM7 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.
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