ArticleMolecular biology of the cell2016
Oms1 associates with cytochrome c oxidase assembly intermediates to stabilize newly synthesized Cox1.
Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 5 citations in OpenAlex.
- An avoidance segment resolves a lethal nuclear-mitochondrial targeting conflict during ribosome assembly.Nature cell biology · 2025Article
- Metabolic shift underlies recovery in reversible infantile respiratory chain deficiency.The EMBO journal · 2020Article
- The human Obg protein GTPBP10 is involved in mitoribosomal biogenesis.Nucleic acids research · 2018Article
- The mitochondrial TMEM177 associates with COX20 during COX2 biogenesis.Biochimica et biophysica acta. Molecular cell research · 2018Article
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mitochondrial cytochrome c oxidase assembles in the inner membrane from subunits of dual genetic origin. The assembly process of the enzyme is initiated by membrane insertion of the mitochondria-encoded Cox1 subunit. During complex maturation, transient assembly intermediates, consisting of structural subunits and specialized chaperone-like assembly factors, are formed. In addition, cofactors such as heme and copper have to be inserted into the nascent complex. To regulate the assembly process, the availability of Cox1 is under control of a regulatory feedback cycle in which translation of COX1 mRNA is stalled when assembly intermediates of Cox1 accumulate through inactivation of the translational activator Mss51. Here we isolate a cytochrome c oxidase assembly intermediate in preparatory scale from coa1Δ mutant cells, using Mss51 as bait. We demonstrate that at this stage of assembly, the complex has not yet incorporated the heme a cofactors. Using quantitative mass spectrometry, we define the protein composition of the assembly intermediate and unexpectedly identify the putative methyltransferase Oms1 as a constituent. Our analyses show that Oms1 participates in cytochrome c oxidase assembly by stabilizing newly synthesized Cox1.
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