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Mitochondrial membrane assembly of TMEM70 protein
H. Kratochvílová, K. Hejzlarová, M. Vrbacký, T. Mráček, V. Karbanová, M. Tesařová, A. Gombitová, D. Cmarko, I. Wittig, J. Zeman, J. Houštěk,
Jazyk angličtina Země Nizozemsko
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- buněčné linie MeSH
- imunoelektronová mikroskopie MeSH
- imunoprecipitace MeSH
- lidé MeSH
- membránové proteiny metabolismus MeSH
- mitochondriální membrány metabolismus MeSH
- mitochondriální proteiny metabolismus MeSH
- mitochondriální protonové ATPasy metabolismus MeSH
- multimerizace proteinu * MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
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).
Charles University Prague 1st Faculty of Medicine 12108 Prague Czech Republic
Institute of Physiology Academy of Sciences of the Czech Republic v v i 14220 Prague Czech Republic
Citace poskytuje Crossref.org
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