Expression and processing of the TMEM70 protein
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
20937241
DOI
10.1016/j.bbabio.2010.10.005
PII: S0005-2728(10)00713-9
Knihovny.cz E-resources
- MeSH
- Cell Line MeSH
- Escherichia coli enzymology MeSH
- Fibroblasts enzymology MeSH
- Mass Spectrometry methods MeSH
- Cloning, Molecular MeSH
- DNA, Complementary genetics MeSH
- Kidney enzymology MeSH
- Humans MeSH
- Membrane Proteins chemistry genetics metabolism MeSH
- Mitochondrial Proteins chemistry genetics metabolism MeSH
- Mitochondrial Proton-Translocating ATPases deficiency MeSH
- Mitochondria enzymology MeSH
- Molecular Sequence Data MeSH
- Mice MeSH
- Amino Acid Sequence MeSH
- Sequence Homology, Amino Acid MeSH
- Sequence Alignment MeSH
- Cattle MeSH
- Submitochondrial Particles enzymology MeSH
- Blotting, Western MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Mice MeSH
- Cattle MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- DNA, Complementary MeSH
- Membrane Proteins MeSH
- Mitochondrial Proteins MeSH
- Mitochondrial Proton-Translocating ATPases MeSH
- TMEM70 protein, human MeSH Browser
TMEM70 protein represents a novel ancillary factor of mammalian ATP synthase. We have investigated import and processing of this factor in human cells using GFP- and FLAG-tagged forms of TMEM70 and specific antibodies. TMEM70 is synthesized as a 29kDa precursor protein that is processed to a 21kDa mature form. Immunocytochemical detection of TMEM70 showed mitochondrial colocalization with MitoTracker Red and ATP synthase. Western blot of subcellular fractions revealed the highest signal of TMEM70 in isolated mitochondria and mitochondrial location was confirmed by mass spectrometry analysis. Based on analysis of submitochondrial fractions, TMEM70 appears to be located in the inner mitochondrial membrane, in accordance with predicated transmembrane regions in the central part of the TMEM70 sequence. Two-dimensional electrophoretic analysis did not show direct interaction of TMEM70 with assembled ATP synthase but indicated the presence of dimeric form of TMEM70. No TMEM70 protein could be found in cells and isolated mitochondria from patients with ATP synthase deficiency due to TMEM70 c.317-2A>G mutation thus confirming that TMEM70 biosynthesis is prevented in these patients.
References provided by Crossref.org
TMEM70 deficiency: long-term outcome of 48 patients
