COX15
Cytochrome c oxidase assembly protein COX15 homolog is an enzyme that in humans is encoded by the COX15 gene.[1][2]
Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. This component is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded subunits may function in the regulation and assembly of the complex. This nuclear gene encodes a protein which is not a structural subunit, but may be essential for the biogenesis of COX formation and may function in the hydroxylation of heme O, according to the yeast mutant studies. This protein is predicted to contain 5 transmembrane domains localized in the mitochondrial inner membrane. Alternative splicing of this gene generates several transcript variants diverging in the 3' region including alternate poly A sites. In total, 2 different isoforms are encoded by these variants.[2]
References
- ↑ Petruzzella V, Tiranti V, Fernandez P, Ianna P, Carrozzo R, Zeviani M (Feb 1999). "Identification and characterization of human cDNAs specific to BCS1, PET112, SCO1, COX15, and COX11, five genes involved in the formation and function of the mitochondrial respiratory chain". Genomics 54 (3): 494–504. doi:10.1006/geno.1998.5580. PMID 9878253.
- 1 2 "Entrez Gene: COX15 COX15 homolog, cytochrome c oxidase assembly protein (yeast)".
Further reading
- Kennaway NG, Carrero-Valenzuela RD, Ewart G; et al. (1991). "Isoforms of mammalian cytochrome c oxidase: correlation with human cytochrome c oxidase deficiency". Pediatr. Res. 28 (5): 529–35. doi:10.1203/00006450-199011000-00024. PMID 2175025.
- Jaluria P, Betenbaugh M, Konstantopoulos K, Shiloach J (2008). "Enhancement of cell proliferation in various mammalian cell lines by gene insertion of a cyclin-dependent kinase homolog". BMC Biotechnol. 7: 71. doi:10.1186/1472-6750-7-71. PMC 2164945. PMID 17945021.
- Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Oquendo CE, Antonicka H, Shoubridge EA; et al. (2004). "Functional and genetic studies demonstrate that mutation in the COX15 gene can cause Leigh syndrome". J. Med. Genet. 41 (7): 540–4. doi:10.1136/jmg.2003.017426. PMC 1735852. PMID 15235026.
- Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Antonicka H, Mattman A, Carlson CG; et al. (2003). "Mutations in COX15 Produce a Defect in the Mitochondrial Heme Biosynthetic Pathway, Causing Early-Onset Fatal Hypertrophic Cardiomyopathy". Am. J. Hum. Genet. 72 (1): 101–14. doi:10.1086/345489. PMC 378614. PMID 12474143.
- Barros MH, Carlson CG, Glerum DM, Tzagoloff A (2001). "Involvement of mitochondrial ferredoxin and Cox15p in hydroxylation of heme O". FEBS Lett. 492 (1–2): 133–8. doi:10.1016/S0014-5793(01)02249-9. PMID 11248251.