Expression and processing of the TMEM70 protein
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
20937241
DOI
10.1016/j.bbabio.2010.10.005
PII: S0005-2728(10)00713-9
Knihovny.cz E-zdroje
- MeSH
- buněčné linie MeSH
- Escherichia coli enzymologie MeSH
- fibroblasty enzymologie MeSH
- hmotnostní spektrometrie metody MeSH
- klonování DNA MeSH
- komplementární DNA genetika MeSH
- ledviny enzymologie MeSH
- lidé MeSH
- membránové proteiny chemie genetika metabolismus MeSH
- mitochondriální proteiny chemie genetika metabolismus MeSH
- mitochondriální protonové ATPasy nedostatek MeSH
- mitochondrie enzymologie MeSH
- molekulární sekvence - údaje MeSH
- myši MeSH
- sekvence aminokyselin MeSH
- sekvenční homologie aminokyselin MeSH
- sekvenční seřazení MeSH
- skot MeSH
- submitochondriální částice enzymologie MeSH
- western blotting MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- myši MeSH
- skot MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- komplementární DNA MeSH
- membránové proteiny MeSH
- mitochondriální proteiny MeSH
- mitochondriální protonové ATPasy MeSH
- TMEM70 protein, human MeSH Prohlížeč
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.
Citace poskytuje Crossref.org
TMEM70 deficiency: long-term outcome of 48 patients
