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COX17 cytochrome c oxidase assembly homolog

COX17, Cox17p
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 involved in the recruitment of copper to mitochondria for incorporation into the COX apoenzyme. This protein shares 92% amino acid sequence identity with mouse and rat Cox17 proteins. This gene is no longer considered to be a candidate gene for COX deficiency. A pseudogene COX17P has been found on chromosome 13. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: SCO1, Atx1, CCS, SCO2, CAN
Papers on COX17
A synthetic gene circuit for measuring autoregulatory feedback control.
Carey et al., Barcelona, Spain. In Integr Biol (camb), Feb 2016
We find that RBP Puf3 does not natively participate in any direct or indirect feedback regulation, but that replacing the native 3'UTR with that of COX17 generates an auto-regulatory negative feedback loop which reduces gene expression noise.
Characterization and sub-cellular localization of GalNAc-binding proteins isolated from human hepatic stellate cells.
Li et al., Xi'an, China. In Biochem Biophys Res Commun, Jan 2016
BTF3, COX17, and ATP5A1) responsible for the regulation of protein binding were up-regulated, and those (i.e.
The cytochrome c oxidase biogenesis factor AtCOX17 modulates stress responses in Arabidopsis.
Gonzalez et al., Santa Fe de la Vera Cruz, Argentina. In Plant Cell Environ, Nov 2015
UNASSIGNED: COX17 is a soluble protein from the mitochondrial intermembrane space that participates in the transfer of copper for cytochrome c oxidase (COX) assembly in eukaryotic organisms.
Aberrant expression of copper associated genes after copper accumulation in COMMD1-deficient dogs.
Penning et al., Utrecht, Netherlands. In J Trace Elem Med Biol, 2015
Expression of genes involved in copper metabolism (COX17, CCS, ATOX1, MT1A, CP, ATP7A, ATP7B, ) and oxidative stress (SOD1, catalase, GPX1 ) was measured by qPCR.
Integrated multi-omics analyses reveal the pleiotropic nature of the control of gene expression by Puf3p.
Pavitt et al., Manchester, United Kingdom. In Sci Rep, 2014
Extensive studies of its regulation of COX17 demonstrate its role in mRNA decay.
Vascular endothelial growth factor recovers suppressed cytochrome c oxidase activity by restoring copper availability in hypertrophic cardiomyocytes.
Kang et al., Chengdu, China. In Exp Biol Med (maywood), 2014
Western blot analysis showed that protein contents of COX subunit COX-IV and Cu chaperones for COX (COX17, COX11, and SCO2) were decreased in response to PE treatment, and recovered after VEGF treatment.
YCF1-mediated cadmium resistance in yeast is dependent on copper metabolism and antioxidant enzymes.
Lee et al., Lincoln, United States. In Antioxid Redox Signal, 2014
RESULTS: Resistance to excess cadmium and copper of the yeast Saccharomyces cerevisiae, which is conferred by PCA1 and CaCRP1 metal efflux P-type ATPases, respectively, does not rely on known metallochaperones, Atx1p, Ccs1p, and Cox17p.
Carbon source-dependent alteration of Puf3p activity mediates rapid changes in the stabilities of mRNAs involved in mitochondrial function.
Olivas et al., Saint Louis, United States. In Nucleic Acids Res, 2014
However, only COX17 has been established as a target of Puf3p-mediated deadenylation and decapping.
Changes in copper concentrations affect the protein levels but not the mRNA levels of copper chaperones in human umbilical vein endothelial cells.
Kang et al., Chengdu, China. In Metallomics, 2014
Western blot analyses showed that CTR1 silencing or TEPA treatment increased the protein levels of copper chaperone ATOX1 and copper chaperone for superoxide dismutase 1 (CCS-1), but decreased copper chaperone for cytochrome c oxidase (COX17).
Disturbance of copper homeostasis is a mechanism for homocysteine-induced vascular endothelial cell injury.
Kang et al., Chengdu, China. In Plos One, 2012
Hcy also decreased the protein levels of Cu chaperone COX17, which was accompanied by a decrease in the activity of cytochrome c oxidase (CCO) and a collapse of mitochondrial membrane potential.
Functional role of two interhelical disulfide bonds in human Cox17 protein from a structural perspective.
Gallo et al., Sesto Fiorentino, Italy. In J Biol Chem, 2011
Functional role of two interhelical disulfide bonds in human Cox17 protein from a structural perspective.
Redox regulation of SCO protein function: controlling copper at a mitochondrial crossroad.
Leary, Saskatoon, Canada. In Antioxid Redox Signal, 2010
To date, a total of 8 soluble (COX17, COX19, COX23, PET191, CMC1-4) and 3 integral membrane (COX11, SCO1, SCO2) accessory proteins with cysteine-containing domains that reside within the mitochondrial intermembrane space (IMS) have been identified in yeast, all of which have human orthologues.
Knockdown of human COX17 affects assembly and supramolecular organization of cytochrome c oxidase.
Rödel et al., Dresden, Germany. In J Mol Biol, 2009
the absence of Cox17 interferes with copper delivery to Cox2, but not to Cox1.
Mitochondrial copper metabolism and delivery to cytochrome c oxidase.
Barrientos et al., Miami, United States. In Iubmb Life, 2008
Recent studies, mostly performed in the yeast Saccharomyces cerevisiae, have provided new clues about 1) the source of the copper used for COX metallation; 2) the roles of Sco1p and Cox11p, the proteins involved in the direct delivery of copper to the Cu(A) and Cu(B) sites, respectively; 3) the action mechanism of Cox17p, a copper chaperone that provides copper to Sco1p and Cox11p; 4) the existence of at least four Cox17p homologues carrying a similar twin CX(9)C domain suggestive of metal binding, Cox19p, Cox23p, Pet191p and Cmc1p, that could be part of the same pathway; and 5) the presence of a disulfide relay system in the intermembrane space of mitochondria that mediates import of proteins with conserved cysteines motifs such as the CX(9)C characteristic of Cox17p and its homologues.
Mapping the functional interaction of Sco1 and Cox2 in cytochrome oxidase biogenesis.
Winge et al., Salt Lake City, United States. In J Biol Chem, 2008
These studies implicate different surfaces on Sco1 for interaction or function with Cox17 and Cox2.
Mitochondrial copper(I) transfer from Cox17 to Sco1 is coupled to electron transfer.
Palumaa et al., Sesto Fiorentino, Italy. In Proc Natl Acad Sci U S A, 2008
Cu(I)HCox17(2S-S), i.e., the copper-loaded form of the protein, can transfer simultaneously copper(I) and two electrons to the human cochaperone Sco1 (HSco1) in the oxidized state, i.e., with its metal-binding cysteines forming a disulfide bond.
Copper transport systems are involved in multidrug resistance and drug transport.
Akiyama et al., Kagoshima, Japan. In Curr Med Chem, 2007
Subsequently three chaperone proteins, HAH1 (human atx1 homologue 1), Cox17p and CCS (copper chaperone for superoxide dismutase) transport copper to the Golgi apparatus, mitochondria and copper/zinc superoxide dismutase respectively.
Oxidative switches in functioning of mammalian copper chaperone Cox17.
Palumaa et al., Tallinn, Estonia. In Biochem J, 2007
XAS (X-ray absorption spectroscopy) determined that Cu4Cox17 contains a Cu4S6-type copper-thiolate cluster, which may provide safe storage of an excess of copper ions
Redox pathways of the mitochondrion.
Leverich et al., Los Angeles, United States. In Antioxid Redox Signal, 2006
A redox pathway (Mia40p and Erv1p) mediates the import of intermembrane space proteins such as the small Tim proteins, Cox17p, and Cox19p, which have disulfide bonds.
Genotypes and clinical phenotypes in children with cytochrome-c oxidase deficiency.
Tulinius et al., Göteborg, Sweden. In Neuropediatrics, 2003
Furthermore, nuclear DNA was analysed for mutations in the SURF1, SCO2, COX10, and COX17 genes and cases with mtDNA depletion were analysed for mutations in the TK2 gene.
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