COQ1/YBR003W Literature Guide Help

Other names published for COQ1: trans-hexaprenyltranstransferase, YBR003W

COQ1 - Mutants/Phenotypes (20)

ReferenceOther Genes Addressed
Sharifpoor S, et al.  (2012) Functional wiring of the yeast kinome revealed by global analysis of genetic network motifs. Genome Res 22(4):791-801
Ohara K, et al.  (2010) Two solanesyl diphosphate synthases with different subcellular localizations and their respective physiological roles in Oryza sativa. J Exp Bot 61(10):2683-92
Ottosson LG, et al.  (2010) Sulfate Assimilation Mediates Tellurite Reduction and Toxicity in Saccharomyces cerevisiae. Eukaryot Cell 9(10):1635-1647
Osman C, et al.  (2009) The genetic interactome of prohibitins: coordinated control of cardiolipin and phosphatidylethanolamine by conserved regulators in mitochondria. J Cell Biol 184(4):583-96
Hsieh EJ, et al.  (2007) Saccharomyces cerevisiae Coq9 polypeptide is a subunit of the mitochondrial coenzyme Q biosynthetic complex. Arch Biochem Biophys 463(1):19-26
Mollet J, et al.  (2007) Prenyldiphosphate synthase, subunit 1 (PDSS1) and OH-benzoate polyprenyltransferase (COQ2) mutations in ubiquinone deficiency and oxidative phosphorylation disorders. J Clin Invest 117(3):765-72
Zhang NN, et al.  (2006) Multiple signaling pathways regulate yeast cell death during the response to mating pheromones. Mol Biol Cell 17(8):3409-22
Gin P and Clarke CF  (2005) Genetic evidence for a multi-subunit complex in coenzyme Q biosynthesis in yeast and the role of the Coq1 hexaprenyl diphosphate synthase. J Biol Chem 280(4):2676-81
Outten CE, et al.  (2005) Cellular factors required for protection from hyperoxia toxicity in Saccharomyces cerevisiae. Biochem J 388(Pt 1):93-101
Outten CE and Culotta VC  (2003) A novel NADH kinase is the mitochondrial source of NADPH in Saccharomyces cerevisiae. EMBO J 22(9):2015-24
Ran H, et al.  (2003) Human targets of Pseudomonas aeruginosa pyocyanin. Proc Natl Acad Sci U S A 100(24):14315-20
Dimmer KS, et al.  (2002) Genetic basis of mitochondrial function and morphology in Saccharomyces cerevisiae. Mol Biol Cell 13(3):847-53
Kainou T, et al.  (2001) Dimer formation of octaprenyl-diphosphate synthase (IspB) is essential for chain length determination of ubiquinone. J Biol Chem 276(11):7876-83
Hsu AY, et al.  (2000) Genetic evidence for a multi-subunit complex in the O-methyltransferase steps of coenzyme Q biosynthesis. Biochim Biophys Acta 1484(2-3):287-97
Poon WW, et al.  (1999) Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis. J Biol Chem 274(31):21665-72
Okada K, et al.  (1998) Biological significance of the side chain length of ubiquinone in Saccharomyces cerevisiae. FEBS Lett 431(2):241-4
Okada K, et al.  (1997) Cloning of the sdsA gene encoding solanesyl diphosphate synthase from Rhodobacter capsulatus and its functional expression in Escherichia coli and Saccharomyces cerevisiae. J Bacteriol 179(19):5992-8
Okada K, et al.  (1996) Polyprenyl diphosphate synthase essentially defines the length of the side chain of ubiquinone. Biochim Biophys Acta 1302(3):217-23
Ashby MN, et al.  (1992) COQ2 is a candidate for the structural gene encoding para-hydroxybenzoate:polyprenyltransferase. J Biol Chem 267(6):4128-36
Tzagoloff A and Dieckmann CL  (1990) PET genes of Saccharomyces cerevisiae. Microbiol Rev 54(3):211-25