COX11/YPL132W Summary Help

Standard Name COX11
Systematic Name YPL132W
Alias LPI13 , PSO7 1
Feature Type ORF, Verified
Description Protein required for delivery of copper to Cox1p; mitochondrial inner membrane protein; association with mitochondrial ribosomes suggests that copper delivery may occur during translation of Cox1p (2, 3, 4 and see Summary Paragraph)
Name Description Cytochrome c OXidase
Chromosomal Location
ChrXVI:301716 to 302618 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All COX11 GO evidence and references
  View Computational GO annotations for COX11
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 4 genes
Resources
Classical genetics
null
reduction of function
Large-scale survey
null
unspecified
Resources
31 total interaction(s) for 29 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 6
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 1
  • PCA: 3

Genetic Interactions
  • Dosage Growth Defect: 1
  • Dosage Lethality: 3
  • Dosage Rescue: 5
  • Phenotypic Enhancement: 2
  • Phenotypic Suppression: 3
  • Positive Genetic: 1
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 1
  • Synthetic Rescue: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 300
Molecular Weight (Da) 34,044
Isoelectric Point (pI) 8.89
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXVI:301716 to 302618 | ORF Map | GBrowse
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..903 301716..302618 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000006053
SUMMARY PARAGRAPH for COX11

COX11 encodes a mitochondrial inner membrane protein that is essential for assembly of the multisubunit enzyme cytochrome c oxidase, which catalyzes the terminal step in the electron transport chain of cellular respiration. Cox11p is involved in the incorporation of copper into the cytochrome oxidase complex, most likely in the formation of the Cu(B) site of the mitochondrially-encoded Cox1p subunit (4, 5). It is well-conserved, with homologs in bacteria, fungi, plants, and animals (5).

Cox11p is anchored to the mitochondrial inner membrane by a single transmembrane segment (6). Its C terminus, which includes a copper-binding domain, is exposed to the intermembrane space and forms a homodimer that binds two Cu(I) ions (7, 6, 4). Copper is delivered to Cox11p by Cox17p, which acts as a copper chaperone specific for Cox11p and Sco1p (8).

Cox11p also interacts with mitochondrial ribosomes via its N terminus (4), although the importance of this is not clear because the N terminus is apparently not essential for function (5). However, the link between Cox11p function and the mitochondrial translation system appears to be conserved, since both of the two COX11 orthologs in Schizosaccharomyces pombe contain 5' extensions relative to S. cerevisiae COX11 that encode proteins similar to the mitochondrial ribosomal protein Rsm22p (6). Cox11p may assist in copper incorporation into Cox1p in a co-translational manner (4, 5). In keeping with this hypothesis, levels of Cox1p are reduced in a cox11 null mutant (5).

The cox11 null mutant exhibits a respiratory defect, failing to grow on nonfermentable carbon sources due to its inability to assemble cytochrome c oxidase (2). cox11 mutants also display sensitivity to various chemicals including photoactivated psoralens, N-nitrosodiethylamine (NDEA), 1,2:7,8-diepoxyoctane (DEO), and hydrogen peroxide (1, 9, 5). The Cox11p function in hydrogen peroxide resistance is separable from its function in cytochrome c oxidase assembly, since the null mutant is both respiratory deficient and hydrogen peroxide sensitive, while cox11 point mutations that affect its copper-binding sites block respiratory growth without causing hydrogen peroxide sensitivity (10). The hydrogen peroxide sensitive phenotype of the null mutant is likely due to accumulation of a transient heme A3-Cox1p intermediate that confers oxidant sensitivity. The intermediate does not form in the presence of wild-type or mutant Cox11p, even though cytochrome c oxidase is not fully assembled in the cox11 point mutant strain (10).

Last updated: 2007-01-25 Contact SGD

References cited on this page View Complete Literature Guide for COX11
1) Brendel M and Henriques JA  (2001) The pso mutants of Saccharomyces cerevisiae comprise two groups: one deficient in DNA repair and another with altered mutagen metabolism. Mutat Res 489(1):79-96
2) Tzagoloff A, et al.  (1990) Cytochrome oxidase assembly in yeast requires the product of COX11, a homolog of the P. denitrificans protein encoded by ORF3. EMBO J 9(9):2759-64
3) Hiser L, et al.  (2000) Cox11p is required for stable formation of the Cu(B) and magnesium centers of cytochrome c oxidase. J Biol Chem 275(1):619-23
4) Khalimonchuk O, et al.  (2005) Evidence for the association of yeast mitochondrial ribosomes with Cox11p, a protein required for the Cu(B) site formation of cytochrome c oxidase. Curr Genet 47(4):223-33
5) Banting GS and Glerum DM  (2006) Mutational analysis of the Saccharomyces cerevisiae cytochrome c oxidase assembly protein Cox11p. Eukaryot Cell 5(3):568-78
6) Carr HS, et al.  (2005) Functional analysis of the domains in Cox11. J Biol Chem 280(24):22664-9
7) Carr HS, et al.  (2002) Yeast Cox11, a protein essential for cytochrome c oxidase assembly, is a Cu(I)-binding protein. J Biol Chem 277(34):31237-42
8) Horng YC, et al.  (2004) Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome C oxidase. J Biol Chem 279(34):35334-40
9) Pungartnik C, et al.  (2002) Further phenotypic characterization of pso mutants of Saccharomyces cerevisiae with respect to DNA repair and response to oxidative stress. Genet Mol Res 1(1):79-89
10) Khalimonchuk O, et al.  (2007) Evidence for a pro-oxidant intermediate in the assembly of cytochrome oxidase. J Biol Chem 282(24):17442-9