Mitochondrial membrane assembly of TMEM70 protein
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
24576557
DOI
10.1016/j.mito.2014.02.010
PII: S1567-7249(14)00024-5
Knihovny.cz E-resources
- Keywords
- ATP synthase, Biogenesis, Mitochondria, TMEM70,
- MeSH
- Cell Line MeSH
- Microscopy, Immunoelectron MeSH
- Immunoprecipitation MeSH
- Humans MeSH
- Membrane Proteins metabolism MeSH
- Mitochondrial Membranes metabolism MeSH
- Mitochondrial Proteins metabolism MeSH
- Mitochondrial Proton-Translocating ATPases metabolism MeSH
- Protein Multimerization * MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Membrane Proteins MeSH
- Mitochondrial Proteins MeSH
- Mitochondrial Proton-Translocating ATPases MeSH
- TMEM70 protein, human MeSH Browser
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).
References provided by Crossref.org
TMEM70 deficiency: long-term outcome of 48 patients
