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Lot6p from Saccharomyces cerevisiae is a FMN-dependent reductase with a potential role in quinone detoxification

dc.contributor.authorSollner, Sonjaen_US
dc.contributor.authorNebauer, Ruthen_US
dc.contributor.authorEhammer, Heidemarieen_US
dc.contributor.authorPrem, Annaen_US
dc.contributor.authorDeller, Sigriden_US
dc.contributor.authorPalfey, Bruce A.en_US
dc.contributor.authorDaum, Güntheren_US
dc.contributor.authorMacheroux, Peteren_US
dc.date.accessioned2010-06-01T18:43:24Z
dc.date.available2010-06-01T18:43:24Z
dc.date.issued2007-03en_US
dc.identifier.citationSollner, Sonja; Nebauer, Ruth; Ehammer, Heidemarie; Prem, Anna; Deller, Sigrid; Palfey, Bruce A.; Daum, GÜnther; Macheroux, Peter (2007). "Lot6p from Saccharomyces cerevisiae is a FMN-dependent reductase with a potential role in quinone detoxification." FEBS Journal 274(5): 1328-1339. <http://hdl.handle.net/2027.42/71921>en_US
dc.identifier.issn1742-464Xen_US
dc.identifier.issn1742-4658en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/71921
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=17298444&dopt=citationen_US
dc.format.extent447017 bytes
dc.format.extent3109 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.publisherBlackwell Publishing Ltden_US
dc.rights2007 The Authors Journal compilation 2007 FEBSen_US
dc.subject.otherDT-diaphoraseen_US
dc.subject.otherLot6pen_US
dc.subject.otherNQO1en_US
dc.subject.otherQuinone Reductaseen_US
dc.subject.otherRedox Cyclingen_US
dc.titleLot6p from Saccharomyces cerevisiae is a FMN-dependent reductase with a potential role in quinone detoxificationen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationum2 Department of Biological Chemistry, University of Michigan, Ann Arbor, MI, USAen_US
dc.contributor.affiliationother1 Graz University of Technology, Institute of Biochemistry, Graz, Austriaen_US
dc.identifier.pmid17298444en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/71921/1/j.1742-4658.2007.05682.x.pdf
dc.identifier.doi10.1111/j.1742-4658.2007.05682.xen_US
dc.identifier.sourceFEBS Journalen_US
dc.identifier.citedreferenceErnster L ( 1987 ) DT-diaphorase – a historical review. Chemica Scripta 27A, 1 – 13.en_US
dc.identifier.citedreferenceRadjendirane V, Joseph P, Lee Y-H, Kimura S, Klein-Szanto AJP, Gonzalez FJ & Jaiswal AK ( 1998 ) Disruption of the DT diaphorase (NQO1) gene in mice leads to increased menadione toxicity. J Biol Chem 273, 7382 – 7389.en_US
dc.identifier.citedreferenceRoss D, Kepa JK, Winski SL, Beall HD, Anwar A & Siegel D ( 2000 ) NAD(P)H: quinone oxidoreductase 1 (NQO1): Chemoprotection, bioactivation, gene regulation and genetic polymorphisms. Chem-Biol Interact 129, 77 – 97.en_US
dc.identifier.citedreferenceFaig M, Bianchet MA, Talalay P, Chen S, Winski S, Ross D & Amzel LM ( 2000 ) Structures of recombinant human and mouse NAD(P)H: quinone oxidoreductases: species comparison and structural changes with substrate binding and release. Proc Natl Acad Sci USA 97, 3177 – 3182.en_US
dc.identifier.citedreferenceFoster CE, Bianchet MA, Talalay P, Zhao Q & Amzel LM ( 1999 ) Crystal structure of human quinone reductase type 2, a metalloflavoprotein. Biochemistry 38, 9881 – 9886.en_US
dc.identifier.citedreferenceLi R, Bianchet MA, Talalay P & Amzel LM ( 1995 ) The three-dimensional structure of NAD(P)H: quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction. Proc Natl Acad Sci USA 92, 8846 – 8850.en_US
dc.identifier.citedreferenceThorn JM, Barton JD, Dixon NE, Ollis DL & Edwards KJ ( 1995 ) Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH. J Mol Biol 249, 785 – 799.en_US
dc.identifier.citedreferenceBrock BJ & Gold MH ( 1996 ) 1,4-Benzoquinone reductase from the Basidiomycete Phanerochaete chrysosporium: spectral and kinetic analysis. Arch Biochem Biophys 331, 31 – 40.en_US
dc.identifier.citedreferenceProchaska HJ, De Long MJ & Talalay P ( 1985 ) On the mechanisms of induction of cancer-protective enzymes: a unifying proposal. Proc Natl Acad Sci USA 82, 8232 – 8236.en_US
dc.identifier.citedreferenceProchaska HJ & Talalay P ( 1991 ) In Oxidative Stress: Oxidants and Antioxidants ( Sies, H, eds), pp. 195 – 211. Academic Press, London.en_US
dc.identifier.citedreferenceFavreau LV & Pickett CB ( 1991 ) Transcriptional regulation of the rat NAD(P)H: quinone reductase gene: identification of regulatory elements controlling basal level expression and inducible expression by planar aromatic compounds and phenolic antioxidants. J Biol Chem 266, 4556 – 4561.en_US
dc.identifier.citedreferenceDenison MS & Fisher JM ( 1988 ) The DNA recognition site for the dioxin-Ah receptor complex: nucleotide sequence and functional analysis. J Biol Chem 263, 17221 – 17224.en_US
dc.identifier.citedreferenceZhang L, Ohta A, Horiuchi H, Takagi M & Imai R ( 2001 ) Multiple mechanisms regulate expression of low temperature responsive (LOT) genes in Saccharomyces cerevisiae. Biochem Biophys Res Commun 283, 531 – 535.en_US
dc.identifier.citedreferenceLiger D, Graille M, Zhou CZ, Leulliot N, Quevillon-Cheruel S, Blondeau K, Janin J & van Tilbeurgh H ( 2004 ) Crystal structure and functional characterization of yeast YLR011wp, an enzyme with NAD(P)H-FMN and ferric iron reductase activities. J Biol Chem 279, 34890 – 34897.en_US
dc.identifier.citedreferenceDeller S, Sollner S, Trenker-El-Toukhy R, Jelesarov I, GÜbitz GM & Macheroux P ( 2006 ) Characterization of a thermostable NADPH: FMN oxidoreductase from the mesophilic bacterium Bacillus subtilis. Biochemistry 45, 7083 – 7091.en_US
dc.identifier.citedreferenceWinzeler EA, Shoemaker DD, Astromoff A, Liang H, Anderson K, Andre B, Bangham R, Benito R, Boeke JD, Bussey H, et al. ( 1999 ) Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis. Science 285, 901 – 906.en_US
dc.identifier.citedreferenceDaum G, BÖhni PC & Schatz G ( 1982 ) Import of proteins into mitochondria: cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria, J Biol Chem 257, 13028 – 13033.en_US
dc.identifier.citedreferenceZinser E, Sperka-Gottlieb CDM, Fasch E-V, Kohlwein SD, Paltauf F & Daum G ( 1991 ) Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae. J Bacteriol 173, 2026 – 2034.en_US
dc.identifier.citedreferenceHurt EC, McDowall A & Schimmang T ( 1988 ) Nucleolar and nuclear envelope proteins of the yeast Saccharomyces cerevisiae. Eur J Cell Biol 46, 554 – 563.en_US
dc.identifier.citedreferenceAris JP & Blobel G ( 1991 ) Isolation of yeast nuclei. Methods Enzymol 194, 735 – 749.en_US
dc.identifier.citedreferenceUchida E, Ohsumi Y & Anraku Y ( 1988 ) Purification of yeast vacuolar membrane H + -ATPase and enzymological discrimination of three ATP-driven proton pumps in Saccharomyces cerevisiae. Methods Enzymol 157, 544 – 562.en_US
dc.identifier.citedreferenceSerrano R ( 1988 ) H + -ATPase from plasma membranes of Saccharomyces cerevisiae and Avena sativa roots: purification and reconstitution. Methods Enzymol 157, 523 – 544.en_US
dc.identifier.citedreferenceZinser E & Daum G ( 1995 ) Isolation and biochemical characterization of organelles from the yeast Saccharomyces cerevisiae. Yeast 11, 493 – 536.en_US
dc.identifier.citedreferenceLowry OH, Rosebrough NJ, Farr AL & Randall RJ ( 1951 ) Protein measurement with the folin phenol reagent. J Biol Chem 193, 265 – 275.en_US
dc.identifier.citedreferenceLaemmli UK ( 1970 ) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680 – 685.en_US
dc.identifier.citedreferenceHaid A & Suissa M ( 1983 ) Immunochemical identification of membrane proteins after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Methods Enzymol 96, 192 – 205.en_US
dc.identifier.citedreferenceLongtine MS, McKenzie A, Demarini DJ, Shah NG, Wach A, Brachat A, Philippsen P & Pringle JR ( 1998 ) Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerervisiae. Yeast 14, 953 – 961.en_US
dc.identifier.citedreferenceGietz D, St. Jean A, Woods RA & Schiestl RH ( 1992 ) Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res 20, 1425.en_US
dc.identifier.citedreferenceRodriguez CE, Shinyashiki M, Froines JYuRC, Fukuto JM & Cho AK ( 2004 ) An examination of quinone toxicity using the yeast Saccharomyces cerevisiae model system. Toxicology 201, 185 – 196.en_US
dc.identifier.citedreferenceMassey V ( 1990 ) Flavin and Flavoproteins ( Curti, B, Ronchi, S, & & Zanetti, G, eds), pp. 59 – 66. Walter de Gruyter & Co, Berlin.en_US
dc.identifier.citedreferenceKumar A, Agarwal S, Heyman JA, Matson S, Heidtman M, Piccirillo S, Umansky L, Drawid A, Jansen R, Liu Y, et al. ( 2002 ) Subcellular localization of the yeast proteome. Genes Dev 16, 707 – 719.en_US
dc.identifier.citedreferenceHuh W-K, Falvo JV, Gerke LC, Carroll AS, Howson RW, Weissman JS & O'Shea EK ( 2003 ) Global analysis of protein localization in budding yeast. Nature 425, 686 – 691.en_US
dc.identifier.citedreferenceMÜller O ( 1942 ) Oxidation–reduction potentials measured with the dropping mercury electrode. J Biol Chem 145, 425 – 441.en_US
dc.identifier.citedreferenceMinnaert K ( 1965 ) Measurement of the equilibrium constant of the reaction between cytochrome c and cytochrome a. Biochim Biophys Acta 110, 42 – 56.en_US
dc.identifier.citedreferenceSuzuki Y, Yoda T, Ruhul A & Sugiura W ( 2001 ) Molecular cloning and characterization of the gene coding for azoreductase from Bacillus sp. OY1-2 isolated from soil. J Biol Chem 276, 9059 – 9065.en_US
dc.identifier.citedreferenceTrost P, Bonora P, Scagliarini S & Pupillo P ( 1995 ) Purification and properties of NAD(P)H: (quinone-acceptor) oxidoreductase of sugarbeet cells. Eur J Biochem 234, 452 – 458.en_US
dc.identifier.citedreferenceZhou Z, Fisher D, Spidel J, Greenfield J, Patson B, Fazal A, Wigal C, Moe OA & Madura JD ( 2003 ) Kinetic and docking studies of the interaction of quinones with the quinone reductase active site. Biochemistry 42, 1985 – 1994.en_US
dc.identifier.citedreferenceIyanagi T ( 1987 ) On the mechanisms of one- and two-electron transfer by flavin enzymes. Chemica Scripta 27A, 31 – 36.en_US
dc.identifier.citedreferenceTedeschi G, Chen S & Massey V ( 1995 ) DT-diaphorase: redox potential, steady-state, and rapid reaction studies. J Biol Chem 270, 1198 – 1204.en_US
dc.identifier.citedreferencePrestera T, Prochaska HJ & Talalay P ( 1992 ) Inhibition of NAD(P)H: (quinone-acceptor) oxidoreductase by cibacron blue and related anthraquinone dyes: a structure–activity study. Biochemistry 31, 824 – 833.en_US
dc.identifier.citedreferenceHosoda S, Nakamura W & Hayashi K ( 1974 ) Properties and reaction mechanism of DT diaphorase from rat liver. J Biol Chem 249, 6416 – 6423.en_US
dc.identifier.citedreferenceAsher G, Dym O, Tsvetkov P, Adler J & Shaul Y ( 2006 ) The crystal structure of NAD(P)H quinone oxidoreductase 1 in complex with its potent inhibitor dicoumarol. Biochemistry 45, 6372 – 6378.en_US
dc.identifier.citedreferenceSoballe B & Poole RK ( 1999 ) Microbial ubiquinones: multiple roles in respiration, gene regulation and oxidative stress management. Microbiology 145, 1817 – 1830.en_US
dc.identifier.citedreferenceAsher G, Tsvetkov P, Kahana C & Shaul Y ( 2005 ) A mechanism of ubiquitin-independent proteasomal degradation of the tumor suppressors p53 and p73. Genes Dev 19, 316 – 321.en_US
dc.identifier.citedreferenceVolland C, Urban-Grimal D, Geraud G & Haguenauer-Tsapis R ( 1994 ) Endocytosis and degradation of the yeast uracil permease under adverse conditions. J Biol Chem 269, 9833 – 9841.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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