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TMEM70 functions in the assembly of complexes I and V.
- Source :
-
Biochimica et biophysica acta. Bioenergetics [Biochim Biophys Acta Bioenerg] 2020 Aug 01; Vol. 1861 (8), pp. 148202. Date of Electronic Publication: 2020 Apr 07. - Publication Year :
- 2020
-
Abstract
- Protein complexes from the oxidative phosphorylation (OXPHOS) system are assembled with the help of proteins called assembly factors. We here delineate the function of the inner mitochondrial membrane protein TMEM70, in which mutations have been linked to OXPHOS deficiencies, using a combination of BioID, complexome profiling and coevolution analyses. TMEM70 interacts with complex I and V and for both complexes the loss of TMEM70 results in the accumulation of an assembly intermediate followed by a reduction of the next assembly intermediate in the pathway. This indicates that TMEM70 has a role in the stability of membrane-bound subassemblies or in the membrane recruitment of subunits into the forming complex. Independent evidence for a role of TMEM70 in OXPHOS assembly comes from evolutionary analyses. The TMEM70/TMEM186/TMEM223 protein family, of which we show that TMEM186 and TMEM223 are mitochondrial in human as well, only occurs in species with OXPHOS complexes. Our results validate the use of combining complexome profiling with BioID and evolutionary analyses in elucidating congenital defects in protein complex assembly.<br />Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.<br /> (Copyright © 2020 The Authors. Published by Elsevier B.V. All rights reserved.)
- Subjects :
- Biotinylation
Evolution, Molecular
Gene Knockout Techniques
HEK293 Cells
Humans
Membrane Proteins deficiency
Membrane Proteins genetics
Mitochondrial Proteins deficiency
Mitochondrial Proteins genetics
Oxidative Phosphorylation
Protein Binding
Electron Transport Complex I metabolism
Membrane Proteins metabolism
Mitochondrial Proteins metabolism
Mitochondrial Proton-Translocating ATPases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1879-2650
- Volume :
- 1861
- Issue :
- 8
- Database :
- MEDLINE
- Journal :
- Biochimica et biophysica acta. Bioenergetics
- Publication Type :
- Academic Journal
- Accession number :
- 32275929
- Full Text :
- https://doi.org/10.1016/j.bbabio.2020.148202