메뉴 건너뛰기




Volumn 30, Issue 3, 2013, Pages 602-612

Functional evolution of an anthocyanin pathway enzyme during a flower color transition

Author keywords

ancestral state reconstruction; anthocyanins; dihydroflavonol 4 reductase; flower color; Iochroma

Indexed keywords

ANTHOCYANIN; VEGETABLE PROTEIN;

EID: 84873571934     PISSN: 07374038     EISSN: 15371719     Source Type: Journal    
DOI: 10.1093/molbev/mss255     Document Type: Article
Times cited : (48)

References (50)
  • 1
    • 37549017103 scopus 로고    scopus 로고
    • Convergence and parallelism reconsidered: What have we learned about the genetics of adaptation?
    • Arendt J, Reznick D. 2008. Convergence and parallelism reconsidered: what have we learned about the genetics of adaptation? Trends Ecol Evol. 23:26-32.
    • (2008) Trends Ecol Evol , vol.23 , pp. 26-32
    • Arendt, J.1    Reznick, D.2
  • 2
    • 0024769577 scopus 로고
    • Flavonoid synthesis in Petunia hybrida-partial characterization of dihydroflavonol-4-reductase genes
    • Beld M, Martin C, Huits H, Stuitje AR, Gerats AGM. 1989. Flavonoid synthesis in Petunia hybrida-partial characterization of dihydroflavonol-4- reductase genes. Plant Mol Biol. 13:491-502.
    • (1989) Plant Mol Biol , vol.13 , pp. 491-502
    • Beld, M.1    Martin, C.2    Huits, H.3    Stuitje, A.R.4    Gerats, A.G.M.5
  • 3
    • 78650005340 scopus 로고    scopus 로고
    • Lack of evidence for sign epistasis between beneficial mutations in an RNA bacteriophage
    • Betancourt A. 2010. Lack of evidence for sign epistasis between beneficial mutations in an RNA bacteriophage. J Mol Evol. 71:437-443.
    • (2010) J Mol Evol , vol.71 , pp. 437-443
    • Betancourt, A.1
  • 4
    • 0036036258 scopus 로고    scopus 로고
    • Phylogenetics of asterids based on 3 coding and 3 non-coding chloroplast DNA markers and the utility of non-coding DNA at higher taxonomic levels
    • Bremer B, Bremer K, Heidari N, Erixon P, Olmstead RG, Anderberg AA, Kallersjo M, Barkhordarian E. 2002. Phylogenetics of asterids based on 3 coding and 3 non-coding chloroplast DNA markers and the utility of non-coding DNA at higher taxonomic levels. Mol Phylogenet Evol. 24:274-301.
    • (2002) Mol Phylogenet Evol , vol.24 , pp. 274-301
    • Bremer, B.1    Bremer, K.2    Heidari, N.3    Erixon, P.4    Olmstead, R.G.5    Anderberg, A.A.6    Kallersjo, M.7    Barkhordarian, E.8
  • 5
    • 70349464621 scopus 로고    scopus 로고
    • An epistatic ratchet constrains the direction of glucocorticoid receptor evolution
    • Bridgham JT, Ortlund EA, Thornton JW. 2009. An epistatic ratchet constrains the direction of glucocorticoid receptor evolution. Nature 461:515-519.
    • (2009) Nature , vol.461 , pp. 515-519
    • Bridgham, J.T.1    Ortlund, E.A.2    Thornton, J.W.3
  • 6
    • 74549118236 scopus 로고    scopus 로고
    • Adaptive evolution of pelvic reduction in sticklebacks by recurrent deletion of a Pitx1 enhancer
    • (16 co-authors)
    • Chan YF, Marks ME, Jones FC, et al. (16 co-authors). 2010. Adaptive evolution of pelvic reduction in sticklebacks by recurrent deletion of a Pitx1 enhancer. Science 327:302-305.
    • (2010) Science , vol.327 , pp. 302-305
    • Chan, Y.F.1    Marks, M.E.2    Jones, F.C.3
  • 7
    • 79957958115 scopus 로고    scopus 로고
    • Diminishing returns epistasis among beneficial mutations decelerates adaptation
    • Chou HH, Chiu HC, Delaney NF, Segre D, Marx CJ. 2011. Diminishing returns epistasis among beneficial mutations decelerates adaptation. Science 332:1190-1192.
    • (2011) Science , vol.332 , pp. 1190-1192
    • Chou, H.H.1    Chiu, H.C.2    Delaney, N.F.3    Segre, D.4    Marx, C.J.5
  • 8
    • 34548018528 scopus 로고    scopus 로고
    • Mechanistic approaches to the study of evolution: The functional synthesis
    • Dean AM, Thornton JW. 2007. Mechanistic approaches to the study of evolution: the functional synthesis. Nat Rev Genet. 8:675-688.
    • (2007) Nat Rev Genet , vol.8 , pp. 675-688
    • Dean, A.M.1    Thornton, J.W.2
  • 9
    • 49649114289 scopus 로고    scopus 로고
    • Escape from adaptive conflict after duplication in an anthocyanin pathway gene
    • Des Marais DL, Rausher MD. 2008. Escape from adaptive conflict after duplication in an anthocyanin pathway gene. Nature 454:762-765.
    • (2008) Nature , vol.454 , pp. 762-765
    • Des Marais, D.L.1    Rausher, M.D.2
  • 11
    • 0345700352 scopus 로고    scopus 로고
    • Molecular cloning, substrate specificity of the functionally expressed dihydroflavonol 4-reductases from Malus domestica and Pyrus communis cultivars and the consequences for flavonoid metabolism
    • Fischer TC, Halbwirth H,Meisel B, Stich K, Forkmann G. 2003. Molecular cloning, substrate specificity of the functionally expressed dihydroflavonol 4-reductases from Malus domestica and Pyrus communis cultivars and the consequences for flavonoid metabolism. Arch Biochem Biophys. 412:223-230.
    • (2003) Arch Biochem Biophys , vol.412 , pp. 223-230
    • Fischer, T.C.1    Halbwirth, H.2    Meisel, B.3    Stich, K.4    Forkmann, G.5
  • 12
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N, Peitsch MC. 1997. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18: 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 13
    • 0344951168 scopus 로고    scopus 로고
    • Biochemical formation of anthocyanins in silk tissue of Zea mays
    • Halbwirth H, Martens S, Wienand U, Forkmann G, Stich K. 2003. Biochemical formation of anthocyanins in silk tissue of Zea mays. Plant Sci. 164:489-495.
    • (2003) Plant Sci , vol.164 , pp. 489-495
    • Halbwirth, H.1    Martens, S.2    Wienand, U.3    Forkmann, G.4    Stich, K.5
  • 15
    • 0028814339 scopus 로고
    • Genetics and biochemistry of anthocyanin biosynthesis
    • Holton TA, Cornish EC. 1995. Genetics and biochemistry of anthocyanin biosynthesis. Plant Cell 7:1071-1083.
    • (1995) Plant Cell , vol.7 , pp. 1071-1083
    • Holton, T.A.1    Cornish, E.C.2
  • 16
    • 0035115023 scopus 로고    scopus 로고
    • Alteration of a single amino acid changes the substrate specificity of dihydroflavonol 4-reductase
    • Johnson ET, Ryu S, Yi HK, Shin B, Cheong H, Choi G. 2001. Alteration of a single amino acid changes the substrate specificity of dihydroflavonol 4-reductase. Plant J. 25:325-333.
    • (2001) Plant J , vol.25 , pp. 325-333
    • Johnson, E.T.1    Ryu, S.2    Yi, H.K.3    Shin, B.4    Cheong, H.5    Choi, G.6
  • 17
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones DT, Taylor WR, Thornton JM. 1992. The rapid generation of mutation data matrices from protein sequences. Comput Appl Biosci. 8: 275-282.
    • (1992) Comput Appl Biosci , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 18
    • 79957948242 scopus 로고    scopus 로고
    • Negative epistasis between beneficial mutations in an evolving bacterial population
    • Khan AI, Dinh DM, Schneider D, Lenski RE, Cooper TF. 2011. Negative epistasis between beneficial mutations in an evolving bacterial population. Science 332:1193-1196.
    • (2011) Science , vol.332 , pp. 1193-1196
    • Khan, A.I.1    Dinh, D.M.2    Schneider, D.3    Lenski, R.E.4    Cooper, T.F.5
  • 19
    • 79955590028 scopus 로고    scopus 로고
    • Reciprocal sign epistasis between frequently experimentally evolved adaptive mutations causes a rugged fitness landscape
    • Kvitek DJ, Sherlock G. 2011. Reciprocal sign epistasis between frequently experimentally evolved adaptive mutations causes a rugged fitness landscape. Plos Genet. 7:e1002056.
    • (2011) Plos Genet , vol.7
    • Kvitek, D.J.1    Sherlock, G.2
  • 20
    • 42049108931 scopus 로고    scopus 로고
    • Characterization of dihydroflavonol 4-reductases for recombinant plant pigment biosynthesis applications
    • Leonard E, Yan Y, Chemler J, Matern U, Martens S, Koffas MAG. 2008. Characterization of dihydroflavonol 4-reductases for recombinant plant pigment biosynthesis applications. Biocatal Biotransfor. 26: 243-251.
    • (2008) Biocatal Biotransfor , vol.26 , pp. 243-251
    • Leonard, E.1    Yan, Y.2    Chemler, J.3    Matern, U.4    Martens, S.5    Koffas, M.A.G.6
  • 23
    • 0030612598 scopus 로고    scopus 로고
    • A single amino acid substitution converts a carboxylesterase to an organophosphorus hydrolase and confers insecticide resistance on a blowfly
    • Newcomb RD, Campbell PM, Ollis DL, Cheah E, Russell RJ, Oakeshott JG. 1997. A single amino acid substitution converts a carboxylesterase to an organophosphorus hydrolase and confers insecticide resistance on a blowfly. Proc Natl Acad Sci USA. 94:7464-7468.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7464-7468
    • Newcomb, R.D.1    Campbell, P.M.2    Ollis, D.L.3    Cheah, E.4    Russell, R.J.5    Oakeshott, J.G.6
  • 24
    • 0003009508 scopus 로고    scopus 로고
    • Phylogeny and provisional classification of the Solanaceae based on chloroplast DNA
    • Nee M, Symon DE, Lester RN, Jessop JP, editors Kew (United Kingdom): Royal Botanical Gardens
    • Olmstead RC, Sweere JA, Spangler RE, Bohs L, Palmer JD. 1999. Phylogeny and provisional classification of the Solanaceae based on chloroplast DNA. In: Nee M, Symon DE, Lester RN, Jessop JP, editors. Solanaceae IV. Kew (United Kingdom): Royal Botanical Gardens. p. 111-137.
    • (1999) Solanaceae IV , pp. 111-137
    • Olmstead, R.C.1    Sweere, J.A.2    Spangler, R.E.3    Bohs, L.4    Palmer, J.D.5
  • 26
    • 34548040966 scopus 로고    scopus 로고
    • Crystal structure of an ancient protein: Evolution by conformational epistasis
    • Ortlund EA, Bridgham JT, Redinbo MR, Thornton JW. 2007. Crystal structure of an ancient protein: evolution by conformational epistasis. Science 317:1544-1548.
    • (2007) Science , vol.317 , pp. 1544-1548
    • Ortlund, E.A.1    Bridgham, J.T.2    Redinbo, M.R.3    Thornton, J.W.4
  • 27
    • 82955229552 scopus 로고    scopus 로고
    • Impact of epistasis and pleiotropy on evolutionary adaptation
    • Ostman B, Hintze A, Adami C. 2012. Impact of epistasis and pleiotropy on evolutionary adaptation. Proc Biol Sci. 279:247-256.
    • (2012) Proc Biol Sci , vol.279 , pp. 247-256
    • Ostman, B.1    Hintze, A.2    Adami, C.3
  • 31
    • 54149088214 scopus 로고    scopus 로고
    • Epistasis - The essential role of gene interactions in the structure and evolution of genetic systems
    • Phillips PC. 2008. Epistasis-the essential role of gene interactions in the structure and evolution of genetic systems. Nat Rev Genet. 9: 855-867.
    • (2008) Nat Rev Genet , vol.9 , pp. 855-867
    • Phillips, P.C.1
  • 35
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • Ronquist F, Huelsenbeck JP. 2003. MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 19:1572-1574.
    • (2003) Bioinformatics , vol.19 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 36
    • 0030830534 scopus 로고    scopus 로고
    • Mutation and extinction: The role of variable mutational effects, synergistic epistasis, beneficial mutations, and degree of outcrossing
    • Schultz ST, Lynch M. 1997. Mutation and extinction: the role of variable mutational effects, synergistic epistasis, beneficial mutations, and degree of outcrossing. Evolution 51:1363-1371.
    • (1997) Evolution , vol.51 , pp. 1363-1371
    • Schultz, S.T.1    Lynch, M.2
  • 38
    • 33748370128 scopus 로고    scopus 로고
    • Phylogenetics of the florally diverse Andean clade Iochrominae (Solanaceae)
    • Smith SD, Baum DA. 2006. Phylogenetics of the florally diverse Andean clade Iochrominae (Solanaceae). Am J Bot. 93:1140-1153.
    • (2006) Am J Bot , vol.93 , pp. 1140-1153
    • Smith, S.D.1    Baum, D.A.2
  • 39
    • 80053213787 scopus 로고    scopus 로고
    • Gene loss and parallel evolution contribute to species difference in flower color
    • Smith SD, Rausher MD. 2011. Gene loss and parallel evolution contribute to species difference in flower color.Mol Biol Evol. 28:2799-2810.
    • (2011) Mol Biol Evol , vol.28 , pp. 2799-2810
    • Smith, S.D.1    Rausher, M.D.2
  • 40
    • 0000260062 scopus 로고
    • Enzymic and non-enzymic reduction of (+)-dihydroquercetin to its 3,4-diol
    • Stafford HA, Lester HH. 1982. Enzymic and non-enzymic reduction of (+)-dihydroquercetin to its 3,4-diol. Plant Physiol. 70:695-698.
    • (1982) Plant Physiol , vol.70 , pp. 695-698
    • Stafford, H.A.1    Lester, H.H.2
  • 41
    • 33750403801 scopus 로고    scopus 로고
    • RAxML-VI-HPC: Maximum likelihood-based phylogenetic analyses with thousands of taxa and mixed models
    • Stamatakis A. 2006. RAxML-VI-HPC: maximum likelihood-based phylogenetic analyses with thousands of taxa and mixed models. Bioinformatics 22:2688-2690.
    • (2006) Bioinformatics , vol.22 , pp. 2688-2690
    • Stamatakis, A.1
  • 42
    • 40149100174 scopus 로고    scopus 로고
    • Adaptive variation in beach mice produced by two interacting pigmentation genes
    • (vol 5, pg e219 2007)
    • Steiner CC, Weber JN, Hoekstra HE. 2008. Adaptive variation in beach mice produced by two interacting pigmentation genes (vol 5, pg e219, 2007). Plos Biol. 6:418-418.
    • (2008) Plos Biol , vol.6 , pp. 418-418
    • Steiner, C.C.1    Weber, J.N.2    Hoekstra, H.E.3
  • 44
    • 33645666942 scopus 로고    scopus 로고
    • Darwinian evolution can follow only very few mutational paths to fitter proteins
    • Weinreich DM, Delaney NF, DePristo MA, Hartl DL. 2006. Darwinian evolution can follow only very few mutational paths to fitter proteins. Science 312:111-114.
    • (2006) Science , vol.312 , pp. 111-114
    • Weinreich, D.M.1    Delaney, N.F.2    Depristo, M.A.3    Hartl, D.L.4
  • 45
    • 21044435697 scopus 로고    scopus 로고
    • Perspective: Sign epistasis and genetic constraint on evolutionary trajectories
    • Weinreich DM, Watson RA, Chao L. 2005. Perspective: sign epistasis and genetic constraint on evolutionary trajectories. Evolution 59: 1165-1174.
    • (2005) Evolution , vol.59 , pp. 1165-1174
    • Weinreich, D.M.1    Watson, R.A.2    Chao, L.3
  • 47
    • 1642506289 scopus 로고    scopus 로고
    • Molecular and biochemical analysis of two cDNA clones encoding dihydroflavonol-4-reductase from Medicago truncatula
    • Xie DY, Jackson LA, Cooper JD, Ferreira D, Paiva NL. 2004. Molecular and biochemical analysis of two cDNA clones encoding dihydroflavonol-4-reductase from Medicago truncatula. Plant Physiol. 134:979-994.
    • (2004) Plant Physiol , vol.134 , pp. 979-994
    • Xie, D.Y.1    Jackson, L.A.2    Cooper, J.D.3    Ferreira, D.4    Paiva, N.L.5
  • 48
    • 0031897964 scopus 로고    scopus 로고
    • Likelihood ratio tests for detecting positive selection and application to primate lysozyme evolution
    • Yang ZH. 1998. Likelihood ratio tests for detecting positive selection and application to primate lysozyme evolution. Mol Biol Evol. 15: 568-573.
    • (1998) Mol Biol Evol , vol.15 , pp. 568-573
    • Zh, Y.1
  • 49
    • 34547803197 scopus 로고    scopus 로고
    • PAML 4: Phylogenetic analysis by maximum likelihood
    • Yang ZH. 2007. PAML 4: phylogenetic analysis by maximum likelihood. Mol Biol Evol. 24:1586-1591.
    • (2007) Mol Biol Evol , vol.24 , pp. 1586-1591
    • Zh, Y.1
  • 50
    • 0036270185 scopus 로고    scopus 로고
    • Codon-substitution models for detecting molecular adaptation at individual sites along specific lineages
    • Yang ZH, Nielsen R. 2002. Codon-substitution models for detecting molecular adaptation at individual sites along specific lineages. Mol Biol Evol. 19:908-917.
    • (2002) Mol Biol Evol , vol.19 , pp. 908-917
    • Zh, Y.1    Nielsen, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.