ArticleThe Journal of biological chemistry2012
Oligomerization of heme o synthase in cytochrome oxidase biogenesis is mediated by cytochrome oxidase assembly factor Coa2.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 25 citations in OpenAlex.
- Molecular analysis of a new patient COX15 mutation provides insight into the etiology of fatal infantile cardioencephalopathy.The Journal of biological chemistry · 2026Article
- Mechanisms of heme transport in the mitochondria.Biochemical Society transactions · 2025Review
- More than Just Bread and Wine: Using Yeast to Understand Inherited Cytochrome Oxidase Deficiencies in Humans.International journal of molecular sciences · 2024Review
- Biosynthesis and trafficking of hemeCritical reviews in biochemistry and molecular biology · 2021Review
- Review
- Article
- Mitochondrial OXPHOS Biogenesis: Co-Regulation of Protein Synthesis, Import, and Assembly Pathways.International journal of molecular sciences · 2020Review
- Review
- Arabidopsis mtHSC70-1 physically interacts with the Cox2 subunit of cytochromePlant signaling & behavior · 2020Article
- Cox15 interacts with the cytochromeThe Journal of biological chemistry · 2018Article
- Mitochondrial cytochrome c oxidase biogenesis: Recent developments.Seminars in cell & developmental biology · 2018Review
- The Complexity of Mitochondrial Complex IV: An Update of Cytochrome c Oxidase Biogenesis in Plants.International journal of molecular sciences · 2018Review
- The Cox1 C-terminal domain is a central regulator of cytochromeThe Journal of biological chemistry · 2017Article
- AEMBO reports · 2017Article
- The Assembly Factor Pet117 Couples Heme a Synthase Activity to Cytochrome Oxidase Assembly.The Journal of biological chemistry · 2017Article
- Analysis of Oligomerization Properties of Heme a Synthase Provides Insights into Its Function in Eukaryotes.The Journal of biological chemistry · 2016Article
- A Novel Function of Pet54 in Regulation of Cox1 Synthesis in Saccharomyces cerevisiae Mitochondria.The Journal of biological chemistry · 2016Article
- Bringing Bioactive Compounds into Membranes: The UbiA Superfamily of Intramembrane Aromatic Prenyltransferases.Trends in biochemical sciences · 2016Review
- Quality control of mitochondrial protein synthesis is required for membrane integrity and cell fitness.The Journal of cell biology · 2015Article
- The heme a synthase Cox15 associates with cytochrome c oxidase assembly intermediates during Cox1 maturation.Molecular and cellular biology · 2013Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The synthesis of the heme a cofactor used in cytochrome c oxidase (CcO) is dependent on the sequential action of heme o synthase (Cox10) and heme a synthase (Cox15). The active state of Cox10 appears to be a homo-oligomeric complex, and formation of this complex is dependent on the newly synthesized CcO subunit Cox1 and the presence of an early Cox1 assembly intermediate. Cox10 multimerization is triggered by progression of Cox1 from the early assembly intermediate to downstream intermediates. The CcO assembly factor Coa2 appears important in coupling the presence of newly synthesized Cox1 to Cox10 oligomerization. Cells lacking Coa2 are impaired in Cox10 complex formation as well as the formation of a high mass Cox15 complex. Increasing Cox1 synthesis in coa2Δ cells restores respiratory function if Cox10 protein levels are elevated. The C-terminal segment of Cox1 is important in triggering Cox10 oligomerization. Expression of the C-terminal 54 residues of Cox1 appended to a heterologous matrix protein leads to efficient Cox10 complex formation in coa2Δ cells, but it fails to induce Cox15 complex formation. The state of Cox10 was evaluated in mutants, which predispose human patients to CcO deficiency and the neurological disorder Leigh syndrome. The presence of the D336V mutation in the yeast Cox10 backbone results in a catalytically inactive enzyme that is fully competent to oligomerize. Thus, Cox10 oligomerization and catalytic activation are separate processes and can be uncoupled.
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