COX3/Q0275 Literature Guide Help

Other names published for COX3: OXI2, cytochrome c oxidase subunit 3, Q0275

COX3 - Mutants/Phenotypes (23)

ReferenceOther Genes Addressed
Elliott LE, et al.  (2012) Multiple roles of the Cox20 chaperone in assembly of Saccharomyces cerevisiae cytochrome c oxidase. Genetics 190(2):559-67
Bourges I, et al.  (2009) Multiple defects in the respiratory chain lead to the repression of genes encoding components of the respiratory chain and TCA cycle enzymes. J Mol Biol 387(5):1081-91
Herst PM, et al.  (2008) Plasma membrane electron transport in Saccharomyces cerevisiae depends on the presence of mitochondrial respiratory subunits. FEMS Yeast Res 8(6):897-905
Khalimonchuk O, et al.  (2007) Evidence for a pro-oxidant intermediate in the assembly of cytochrome oxidase. J Biol Chem 282(24):17442-9
Cobine PA, et al.  (2006) Mitochondrial matrix copper complex used in metallation of cytochrome oxidase and superoxide dismutase. J Biol Chem 281(48):36552-9
Williams EH, et al.  (2005) Alteration of a novel dispensable mitochondrial ribosomal small-subunit protein, Rsm28p, allows translation of defective COX2 mRNAs. Eukaryot Cell 4(2):337-45
Bratton M, et al.  (2003) Disease-related mutations in cytochrome c oxidase studied in yeast and bacterial models. Eur J Biochem 270(6):1222-30
Meunier B and Taanman JW  (2002) Mutations of cytochrome c oxidase subunits 1 and 3 in Saccharomyces cerevisiae: assembly defect and compensation. Biochim Biophys Acta 1554(1-2):101-7
Meunier B  (2001) Site-directed mutations in the mitochondrially encoded subunits I and III of yeast cytochrome oxidase. Biochem J 354(Pt 2):407-12
Green-Willms NS, et al.  (1998) Functional interactions between yeast mitochondrial ribosomes and mRNA 5' untranslated leaders. Mol Cell Biol 18(4):1826-34
Launhardt H, et al.  (1998) Drug-induced phenotypes provide a tool for the functional analysis of yeast genes. Yeast 14(10):935-42
Wiesenberger G and Fox TD  (1997) Pet127p, a membrane-associated protein involved in stability and processing of Saccharomyces cerevisiae mitochondrial RNAs. Mol Cell Biol 17(5):2816-24
Costanzo MC and Fox TD  (1995) A point mutation in the 5'-untranslated leader that affects translational activation of the mitochondrial COX3 mRNA. Curr Genet 28(1):60-6
Wiesenberger G, et al.  (1995) Analysis of the Saccharomyces cerevisiae mitochondrial COX3 mRNA 5' untranslated leader: translational activation and mRNA processing. Mol Cell Biol 15(6):3291-300
Folley LS and Fox TD  (1994) Reduced dosage of genes encoding ribosomal protein S18 suppresses a mitochondrial initiation codon mutation in Saccharomyces cerevisiae. Genetics 137(2):369-79
Costanzo MC and Fox TD  (1993) Suppression of a defect in the 5' untranslated leader of mitochondrial COX3 mRNA by a mutation affecting an mRNA-specific translational activator protein. Mol Cell Biol 13(8):4806-13
Meunier B, et al.  (1993) Genetic screening in Saccharomyces cerevisiae for large numbers of mitochondrial point mutations which affect structure and function of catalytic subunits of cytochrome-c oxidase. Eur J Biochem 213(1):129-35
Folley LS and Fox TD  (1991) Site-directed mutagenesis of a Saccharomyces cerevisiae mitochondrial translation initiation codon. Genetics 129(3):659-68
Kruszewska A and Szczesniak B  (1985) Functional nuclear suppressor of mitochondrial oxi2 mutations in yeast. Curr Genet 10(2):87-93
Stephenson G, et al.  (1981) mit-Mutations in the structural gene of subunit III of cytochrome oxidase in Saccharomyces cerevisiae. Biochim Biophys Acta 653(3):416-22
Pratje E, et al.  (1979) Sporulation of mitochondrial respiratory deficient mit- mutants of Saccharomyces cerevisiae. Mol Gen Genet 176(3):411-5
Tzagoloff A, et al.  (1975) Assembly of the mitochondrial membrane system. Cytoplasmic mutants of Saccharomyces cerevisiae with lesions in enzymes of the respiratory chain and in the mitochondrial ATPase. J Biol Chem 250(20):8236-42
Ebner E and Schatz G  (1973) Mitochondrial assembly in respiration-deficient mutants of Saccharomyces cerevisiae. 3. A nuclear mutant lacking mitochondrial adenosine triphosphatase. J Biol Chem 248(15):5379-84