Journal
MITOCHONDRION
Volume 15, Issue -, Pages 1-9Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.mito.2014.02.010
Keywords
Mitochondria; ATP synthase; TMEM70; Biogenesis
Categories
Funding
- Grant Agency of the Czech Republic [P303/11/0970, 14-36804G]
- Grant Agency of the Charles University in Prague [37710, 370411]
- Charles University in Prague [PRVOUK P24/ LF1/3, P27/LF1/1, UNCE 204011, 204022]
- Ministry of Education, Youth and Sports of the Czech Republic [LL1204, RVO:67985823]
- L'Oreal-UNESCO fellowship for Women in Science
- Deutsche Forschungsgemeinschaft, Sonderforschungsbereich
- BMBF mitoNET German Network for Mitochondrial Disorders [01GM1113B]
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Dysfunction of TMEM70 disrupts the biogenesis of ATP synthase and represents the frequent cause of autosomal recessive encephalocardiomyopathy. We used tagged forms of TMEM70 and demonstrated that it has a hairpin structure with the N- and C-termini oriented towards the mitochondrial matrix. On BN-PAGE TMEM70 was detected in multiple forms including dimers and displayed partial overlap with assembled ATP synthase. Immunoprecipitation studies confirmed mutual interactions between TMEM70 molecules but, together with immunogold electron microscopy, not direct interaction with ATP synthase subunits. This indicates that the biological function of TMEM70 in the ATP synthase biogenesis may be mediated through interaction with other protein(s). (C) 2014 Elsevier B.V. and Mitochondria Research Society. All rights reserved.
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