메뉴 건너뛰기




Volumn 13, Issue 1, 2013, Pages

Diversification of Quiescin sulfhydryl oxidase in a preserved framework for redox relay

Author keywords

Disulfide bond formation; Flavin adenine dinucleotide; Multi domain; Protein evolution; Thioredoxin

Indexed keywords

AMINO ACID; CATALYSIS; ENZYME ACTIVITY; FUNGUS; NUMERICAL MODEL; PHYLOGENY; PROTEIN; REDOX CONDITIONS; SPECIES DIVERSITY; SUBSTRATE;

EID: 84875033779     PISSN: None     EISSN: 14712148     Source Type: Journal    
DOI: 10.1186/1471-2148-13-70     Document Type: Article
Times cited : (9)

References (30)
  • 1
    • 80052372197 scopus 로고    scopus 로고
    • Multiple ways to make disulfides
    • 10.1016/j.tibs.2011.05.004 21778060
    • Multiple ways to make disulfides. Bulleid NJ, Ellgaard J, Trends Biochem Sci 2011 36 9 485 492 10.1016/j.tibs.2011.05.004 21778060
    • (2011) Trends Biochem Sci , vol.36 , Issue.9 , pp. 485-492
    • Bulleid, N.J.1    Ellgaard, J.2
  • 2
    • 0036715426 scopus 로고    scopus 로고
    • Sulfhydryl oxidases: Emerging catalysts of protein disulfide bond formation in eukaryotes
    • 10.1016/S0003-9861(02)00337-5 12176051
    • Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes. Thorpe C, Hoober K, Raje S, Glynn N, Burnside J, Turi G, Coppock D, Arch Biochem Biophys 2002 405 1 1 12 10.1016/S0003-9861(02)00337-5 12176051
    • (2002) Arch Biochem Biophys , vol.405 , Issue.1 , pp. 1-12
    • Thorpe, C.1    Hoober, K.2    Raje, S.3    Glynn, N.4    Burnside, J.5    Turi, G.6    Coppock, D.7
  • 3
    • 34447313455 scopus 로고    scopus 로고
    • An Arabidopsis quiescin-sulfhydryl oxidase regulates cation homeostasis at the root symplast-xylem interface
    • 10.1038/sj.emboj.7601757 17568770
    • An Arabidopsis quiescin-sulfhydryl oxidase regulates cation homeostasis at the root symplast-xylem interface. Alejandro S, Rodríguez PL, Bellés JM, Yenush L, García-Sanchez MJ, Fernández JA, Serrano R, EMBO J 2007 26 13 3203 3215 10.1038/sj.emboj.7601757 17568770
    • (2007) EMBO J , vol.26 , Issue.13 , pp. 3203-3215
    • Alejandro, S.1    Rodríguez, P.L.2    Bellés, J.M.3    Yenush, L.4    García-Sanchez, M.J.5    Fernández, J.A.6    Serrano, R.7
  • 4
    • 34250787527 scopus 로고    scopus 로고
    • Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1
    • 10.1042/BJ20061510 17331072
    • Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1. Chakravarthi S, Jessop CE, Willer M, Stirling CJ, Bulleid NJ, Biochem J 2007 404 3 403 411 10.1042/BJ20061510 17331072
    • (2007) Biochem J , vol.404 , Issue.3 , pp. 403-411
    • Chakravarthi, S.1    Jessop, C.E.2    Willer, M.3    Stirling, C.J.4    Bulleid, N.J.5
  • 5
    • 16444370823 scopus 로고    scopus 로고
    • Ontogenesis of the sulfhydryl oxidase QSOX expression in rat brain
    • 10.1002/cne.20411 15770657
    • Ontogenesis of the sulfhydryl oxidase QSOX expression in rat brain. Mairet-Coello G, Tury A, Fellmann D, Risold PY, Griffond B, J Comp Neurol 2005 484 4 403 417 10.1002/cne.20411 15770657
    • (2005) J Comp Neurol , vol.484 , Issue.4 , pp. 403-417
    • Mairet-Coello, G.1    Tury, A.2    Fellmann, D.3    Risold, P.Y.4    Griffond, B.5
  • 6
    • 0034673562 scopus 로고    scopus 로고
    • Regulation of the quiescence-induced genes: Quiescin Q6, decorin, and ribosomal protein S29
    • 10.1006/bbrc.2000.2324 10708601
    • Regulation of the quiescence-induced genes: quiescin Q6, decorin, and ribosomal protein S29. Coppock D, Kopman C, Gudas J, Cina-Poppe DA, Biochem Biophys Res Commun 2000 269 2 604 610 10.1006/bbrc.2000.2324 10708601
    • (2000) Biochem Biophys Res Commun , vol.269 , Issue.2 , pp. 604-610
    • Coppock, D.1    Kopman, C.2    Gudas, J.3    Cina-Poppe, D.A.4
  • 7
    • 0032535351 scopus 로고    scopus 로고
    • The quiescin Q6 gene (QSCN6) is a fusion of two ancient gene families: Thioredoxin and ERV1
    • 10.1006/geno.1998.5605 9878249
    • The quiescin Q6 gene (QSCN6) is a fusion of two ancient gene families: thioredoxin and ERV1. Coppock DL, Cina-Poppe D, Gilleran S, Genomics 1998 54 3 460 468 10.1006/geno.1998.5605 9878249
    • (1998) Genomics , vol.54 , Issue.3 , pp. 460-468
    • Coppock, D.L.1    Cina-Poppe, D.2    Gilleran, S.3
  • 8
    • 42449098493 scopus 로고    scopus 로고
    • Human quiescin-sulfhydryl oxidase, QSOX1: Probing internal redox steps by mutagenesis
    • 10.1021/bi702522q
    • Human quiescin-sulfhydryl oxidase, QSOX1: probing internal redox steps by mutagenesis. Heckler EJ, Alon A, Fass D, Thorpe C, Biochem 2008 47 17 4955 4963 10.1021/bi702522q
    • (2008) Biochem , vol.47 , Issue.17 , pp. 4955-4963
    • Heckler, E.J.1    Alon, A.2    Fass, D.3    Thorpe, C.4
  • 10
    • 77951295195 scopus 로고    scopus 로고
    • QSOX contains a pseudo-dimer of functional and degenerate sulfhydryl oxidase domains
    • 10.1016/j.febslet.2010.03.001 20211621
    • QSOX contains a pseudo-dimer of functional and degenerate sulfhydryl oxidase domains. Alon A, Heckler EJ, Thorpe C, Fass D, FEBS Lett 2010 584 8 1521 1525 10.1016/j.febslet.2010.03.001 20211621
    • (2010) FEBS Lett , vol.584 , Issue.8 , pp. 1521-1525
    • Alon, A.1    Heckler, E.J.2    Thorpe, C.3    Fass, D.4
  • 11
    • 41549159471 scopus 로고    scopus 로고
    • The human PDI family: Versatility packed into a single fold
    • 10.1016/j.bbamcr.2007.11.010 18093543
    • The human PDI family: versatility packed into a single fold. Appenzeller-Herzog C, Ellgaard L, Biochim Biophys Acta 2008 1783 4 535 548 10.1016/j.bbamcr.2007.11.010 18093543
    • (2008) Biochim Biophys Acta , vol.1783 , Issue.4 , pp. 535-548
    • Appenzeller-Herzog, C.1    Ellgaard, L.2
  • 12
    • 41449089437 scopus 로고    scopus 로고
    • Generating disulfides with the Quiescin-sulfhydryl oxidases
    • 10.1016/j.bbamcr.2007.10.002 17980160
    • Generating disulfides with the Quiescin-sulfhydryl oxidases. Heckler EJ, Rancy PC, Kodali VK, Thorpe C, Biochim Biophys Acta 2008 1783 4 567 577 10.1016/j.bbamcr.2007.10.002 17980160
    • (2008) Biochim Biophys Acta , vol.1783 , Issue.4 , pp. 567-577
    • Heckler, E.J.1    Rancy, P.C.2    Kodali, V.K.3    Thorpe, C.4
  • 13
    • 0030934272 scopus 로고    scopus 로고
    • The CXXC motif: A rheostat in the active site
    • 10.1021/bi9628580
    • The CXXC motif: a rheostat in the active site. Chivers PT, Prehoda KE, Raines RT, Biochem 1997 36 14 4061 4066 10.1021/bi9628580
    • (1997) Biochem , vol.36 , Issue.14 , pp. 4061-4066
    • Chivers, P.T.1    Prehoda, K.E.2    Raines, R.T.3
  • 14
    • 78650781753 scopus 로고    scopus 로고
    • Comparative genomic study of protein disulfide isomerases from photosynthetic organisms
    • 10.1016/j.ygeno.2010.10.001 20951197
    • Comparative genomic study of protein disulfide isomerases from photosynthetic organisms. Selles B, Jacquot J-P, Rouhier N, Genomics 2011 97 1 37 50 10.1016/j.ygeno.2010.10.001 20951197
    • (2011) Genomics , vol.97 , Issue.1 , pp. 37-50
    • Selles, B.1    Jacquot, J.-P.2    Rouhier, N.3
  • 15
    • 0042921194 scopus 로고    scopus 로고
    • Remarkable interkingdom conservation of intron positions and massive lineage-specific intron loss and gain in eukaryotic evolution
    • 10.1016/S0960-9822(03)00558-X 12956953
    • Remarkable interkingdom conservation of intron positions and massive lineage-specific intron loss and gain in eukaryotic evolution. Rogozin IB, Wolf YI, Sorokin AV, Mirkin BG, Koonin EV, Curr Biol 2003 13 17 1512 1517 10.1016/S0960-9822(03)00558-X 12956953
    • (2003) Curr Biol , vol.13 , Issue.17 , pp. 1512-1517
    • Rogozin, I.B.1    Wolf, Y.I.2    Sorokin, A.V.3    Mirkin, B.G.4    Koonin, E.V.5
  • 16
    • 0029165589 scopus 로고
    • Thioredoxin - A fold for all reasons
    • 10.1016/S0969-2126(01)00154-X 7788290
    • Thioredoxin-a fold for all reasons. Martin JL, Structure 1995 3 3 245 250 10.1016/S0969-2126(01)00154-X 7788290
    • (1995) Structure , vol.3 , Issue.3 , pp. 245-250
    • Martin, J.L.1
  • 17
    • 1642556877 scopus 로고    scopus 로고
    • Snapshots of DsbA in action: Detection of proteins in the process of oxidative folding
    • 10.1126/science.1091724 14739460
    • Snapshots of DsbA in action: detection of proteins in the process of oxidative folding. Kadokura H, Tian H, Zander T, Bardwell JC, Beckwith J, Science 2004 303 5657 534 537 10.1126/science.1091724 14739460
    • (2004) Science , vol.303 , Issue.5657 , pp. 534-537
    • Kadokura, H.1    Tian, H.2    Zander, T.3    Bardwell, J.C.4    Beckwith, J.5
  • 18
    • 34250206320 scopus 로고    scopus 로고
    • A conserved cis-proline precludes metal binding by the active site thiolates in members of the thioredoxin family of proteins
    • 10.1021/bi700152b
    • A conserved cis-proline precludes metal binding by the active site thiolates in members of the thioredoxin family of proteins. Su D, Berndt C, Fomenko DE, Holmgren A, Gladyshev VN, Biochem 2007 46 23 6903 6910 10.1021/bi700152b
    • (2007) Biochem , vol.46 , Issue.23 , pp. 6903-6910
    • Su, D.1    Berndt, C.2    Fomenko, D.E.3    Holmgren, A.4    Gladyshev, V.N.5
  • 19
    • 33747352990 scopus 로고    scopus 로고
    • Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide
    • 10.1016/j.jmb.2006.06.070 16893552
    • Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide. Vitu E, Bentzur M, Lisowsky T, Kaiser CA, Fass D, J Mol Biol 2006 362 1 89 101 10.1016/j.jmb.2006.06.070 16893552
    • (2006) J Mol Biol , vol.362 , Issue.1 , pp. 89-101
    • Vitu, E.1    Bentzur, M.2    Lisowsky, T.3    Kaiser, C.A.4    Fass, D.5
  • 20
    • 0036142325 scopus 로고    scopus 로고
    • A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p
    • 10.1038/nsb740 11740506
    • A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Gross E, Sevier CS, Vala A, Kaiser CA, Fass D, Nat Struct Biol 2002 9 1 61 67 10.1038/nsb740 11740506
    • (2002) Nat Struct Biol , vol.9 , Issue.1 , pp. 61-67
    • Gross, E.1    Sevier, C.S.2    Vala, A.3    Kaiser, C.A.4    Fass, D.5
  • 21
    • 41449101717 scopus 로고    scopus 로고
    • The Erv family of sulfhydryl oxidases
    • 10.1016/j.bbamcr.2007.11.009 18155671
    • The Erv family of sulfhydryl oxidases. Fass D, Biochim Biophys Acta 2008 1783 4 557 566 10.1016/j.bbamcr.2007.11.009 18155671
    • (2008) Biochim Biophys Acta , vol.1783 , Issue.4 , pp. 557-566
    • Fass, D.1
  • 22
    • 80052452886 scopus 로고    scopus 로고
    • Structure of a baculovirus sulfhydryl oxidase, a highly divergent member of the Erv flavoenzyme family
    • 10.1128/JVI.05149-11 21752922
    • Structure of a baculovirus sulfhydryl oxidase, a highly divergent member of the Erv flavoenzyme family. Hakim M, Mandelbaum A, Fass D, J Virol 2011 85 18 9406 9413 10.1128/JVI.05149-11 21752922
    • (2011) J Virol , vol.85 , Issue.18 , pp. 9406-9413
    • Hakim, M.1    Mandelbaum, A.2    Fass, D.3
  • 23
    • 84869497499 scopus 로고    scopus 로고
    • Phylogenetics and enzymology of plant quiescin sulfhydryl oxidase
    • 10.1016/j.febslet.2012.10.003 23068612
    • Phylogenetics and enzymology of plant quiescin sulfhydryl oxidase. Limor-Waisberg K, Alon A, Mehlman T, Fass D, FEBS Lett 2012 586 23 4119 4125 10.1016/j.febslet.2012.10.003 23068612
    • (2012) FEBS Lett , vol.586 , Issue.23 , pp. 4119-4125
    • Limor-Waisberg, K.1    Alon, A.2    Mehlman, T.3    Fass, D.4
  • 24
    • 77749286237 scopus 로고    scopus 로고
    • Quiescin sulfhydryl oxidase from Trypanosoma brucei: Catalytic activity and mechanism of a QSOX family member with a single thioredoxin domain
    • 10.1021/bi902222s
    • Quiescin sulfhydryl oxidase from Trypanosoma brucei: catalytic activity and mechanism of a QSOX family member with a single thioredoxin domain. Kodali VK, Thorpe C, Biochem 2010 49 9 2075 2085 10.1021/bi902222s
    • (2010) Biochem , vol.49 , Issue.9 , pp. 2075-2085
    • Kodali, V.K.1    Thorpe, C.2
  • 25
    • 0034703766 scopus 로고    scopus 로고
    • Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade
    • 10.1016/S0092-8674(00)00180-X 11114333
    • Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade. Katzen F, Beckwith J, Cell 2000 103 5 769 779 10.1016/S0092-8674(00)00180-X 11114333
    • (2000) Cell , vol.103 , Issue.5 , pp. 769-779
    • Katzen, F.1    Beckwith, J.2
  • 26
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • 10.1093/nar/25.24.4876 9396791
    • The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Thomson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG, Nucleic Acids Res 1997 25 4876 4882 10.1093/nar/25.24.4876 9396791
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thomson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 27
    • 84875910520 scopus 로고    scopus 로고
    • Distributed by the author
    • Seattle: University of Washington: Department of Genome Sciences
    • Felsenstein J, PHYLIP (Phylogeny Inference Package) version 3.6 Seattle: University of Washington: Department of Genome Sciences Distributed by the author. 2005
    • (2005) PHYLIP (Phylogeny Inference Package) Version 3.6
    • Felsenstein, J.1
  • 28
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • 10.1006/jmbi.1999.3091 10493868
    • Protein secondary structure prediction based on position-specific scoring matrices. Jones DT, J Mol Biol 1999 292 2 195 202 10.1006/jmbi.1999.3091 10493868
    • (1999) J Mol Biol , vol.292 , Issue.2 , pp. 195-202
    • Jones, D.T.1
  • 29
    • 2142738304 scopus 로고    scopus 로고
    • WebLogo: A sequence logo generator
    • 10.1101/gr.849004 15173120
    • WebLogo: A sequence logo generator. Crooks GE, Hon G, Chandonia JM, Brenner SE, Genome Res 2004 14 1188 1190 10.1101/gr.849004 15173120
    • (2004) Genome Res , vol.14 , pp. 1188-1190
    • Crooks, G.E.1    Hon, G.2    Chandonia, J.M.3    Brenner, S.E.4
  • 30
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • 10.1093/nar/gkq399 20478830
    • ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Ashkenazy H, Erez E, Martz E, Pupko T, Ben-Tal N, Nucleic Acids Res 2010 38 529 W533 10.1093/nar/gkq399 20478830
    • (2010) Nucleic Acids Res , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.