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Volumn 111, Issue 1, 2014, Pages 314-319

Drastic neofunctionalization associated with evolution of the timezyme AANAT 500 Mya

(16)  Falcón, Jack a,b   Coon, Steven L c   Besseau, Laurence a,b   Cazaméa Catalan, Damien a,b   Fuentès, Michaël a,b   Magnanou, Elodie a,b   Paulin, Charles Hubert a,b   Boeuf, Gilles a,b,d   Sauzet, Sandrine a,b   Jørgensen, Even H e   Mazan, Sylvie f   Wolf, Yuri I g   Koonin, Eugene V g   Steinbach, Peter J h   Hyodo, Susumu i   Klein, David C c  

a CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ARALKYLAMINE ACETYLTRANSFERASE; MELATONIN;

EID: 84891930538     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1312634110     Document Type: Article
Times cited : (53)

References (51)
  • 1
    • 0036005756 scopus 로고    scopus 로고
    • The genetic control of eye development and its implications for the evolution of the various eye-types
    • Gehring WJ (2002) The genetic control of eye development and its implications for the evolution of the various eye-types. Int J Dev Biol 46(1): 65-73.
    • (2002) Int J Dev Biol , vol.46 , Issue.1 , pp. 65-73
    • Gehring, W.J.1
  • 2
    • 0033198374 scopus 로고    scopus 로고
    • Pax 6: Mastering eye morphogenesis and eye evolution
    • Gehring WJ, Ikeo K (1999) Pax 6: Mastering eye morphogenesis and eye evolution. Trends Genet 15(9): 371-377.
    • (1999) Trends Genet , vol.15 , Issue.9 , pp. 371-377
    • Gehring, W.J.1    Ikeo, K.2
  • 4
    • 0142216226 scopus 로고    scopus 로고
    • Evolution of photosensory pineal organs in new light: The fate of neuroendocrine photoreceptors
    • Ekström P, Meissl H (2003) Evolution of photosensory pineal organs in new light: The fate of neuroendocrine photoreceptors. Philos Trans R Soc Lond B Biol Sci 358(1438): 1679-1700.
    • (2003) Philos Trans R Soc Lond B Biol Sci , vol.358 , Issue.1438 , pp. 1679-1700
    • Ekström, P.1    Meissl, H.2
  • 5
    • 0024821536 scopus 로고
    • Pineal transducers in the course of evolution: Molecular organization, rhythmic metabolic activity and role
    • Collin JP, et al. (1989) Pineal transducers in the course of evolution: Molecular organization, rhythmic metabolic activity and role. Arch Histol Cytol 52(Suppl): 441-449.
    • (1989) Arch Histol Cytol , vol.52 , Issue.SUPPL. , pp. 441-449
    • Collin, J.P.1
  • 6
    • 0030626244 scopus 로고    scopus 로고
    • The melatonin rhythm-generating enzyme: Molecular regulation of serotonin N-acetyltransferase in the pineal gland
    • Klein DC, et al. (1997) The melatonin rhythm-generating enzyme: Molecular regulation of serotonin N-acetyltransferase in the pineal gland. Recent Prog Horm Res 52: 307-357.
    • (1997) Recent Prog Horm Res , vol.52 , pp. 307-357
    • Klein, D.C.1
  • 7
    • 3242713077 scopus 로고    scopus 로고
    • The 2004 Aschoff/Pittendrigh lecture: Theory of the origin of the pineal gland - A tale of conflict and resolution
    • Klein DC (2004) The 2004 Aschoff/Pittendrigh lecture: Theory of the origin of the pineal gland-a tale of conflict and resolution. J Biol Rhythms 19(4): 264-279.
    • (2004) J Biol Rhythms , vol.19 , Issue.4 , pp. 264-279
    • Klein, D.C.1
  • 8
    • 33646701014 scopus 로고    scopus 로고
    • Evolution of the vertebrate pineal gland: The AANAT hypothesis
    • Klein DC (2006) Evolution of the vertebrate pineal gland: The AANAT hypothesis. Chronobiol Int 23(1-2): 5-20.
    • (2006) Chronobiol Int , vol.23 , Issue.1-2 , pp. 5-20
    • Klein, D.C.1
  • 10
    • 33947510169 scopus 로고    scopus 로고
    • Arylalkylamine N-acetyltransferase: "the timezyme."
    • Klein DC (2007) Arylalkylamine N-acetyltransferase: "The timezyme." J Biol Chem 282(7): 4233-4237.
    • (2007) J Biol Chem , vol.282 , Issue.7 , pp. 4233-4237
    • Klein, D.C.1
  • 11
    • 77953523384 scopus 로고    scopus 로고
    • Mutations of an arylalkylamine-N-acetyltransferase, Bm-iAANAT, are responsible for silkworm melanism mutant
    • Dai FY, et al. (2010) Mutations of an arylalkylamine-N-acetyltransferase, Bm-iAANAT, are responsible for silkworm melanism mutant. J Biol Chem 285(25): 19553-19560.
    • (2010) J Biol Chem , vol.285 , Issue.25 , pp. 19553-19560
    • Dai, F.Y.1
  • 12
    • 0033646107 scopus 로고    scopus 로고
    • Purification, cloning, and characterization of a second arylalkylamine N-acetyltransferase from Drosophila melanogaster
    • Amherd R, Hintermann E, Walz D, Affolter M, Meyer UA (2000) Purification, cloning, and characterization of a second arylalkylamine N-acetyltransferase from Drosophila melanogaster. DNA Cell Biol 19(11): 697-705.
    • (2000) DNA Cell Biol , vol.19 , Issue.11 , pp. 697-705
    • Amherd, R.1    Hintermann, E.2    Walz, D.3    Affolter, M.4    Meyer, U.A.5
  • 13
    • 0035861575 scopus 로고    scopus 로고
    • Characterization of the Saccharomyces cerevisiae homolog of the melatonin rhythm enzyme arylalkylamine N-acetyltransferase (EC 2.3.1.87)
    • Ganguly S, Mummaneni P, Steinbach PJ, Klein DC, Coon SL (2001) Characterization of the Saccharomyces cerevisiae homolog of the melatonin rhythm enzyme arylalkylamine N-acetyltransferase (EC 2.3.1.87). J Biol Chem 276(50): 47239-47247.
    • (2001) J Biol Chem , vol.276 , Issue.50 , pp. 47239-47247
    • Ganguly, S.1    Mummaneni, P.2    Steinbach, P.J.3    Klein, D.C.4    Coon, S.L.5
  • 14
    • 77952497880 scopus 로고    scopus 로고
    • Evolution of AANAT: Expansion of the gene family in the cephalochordate amphioxus
    • Pavlicek J, et al. (2010) Evolution of AANAT: Expansion of the gene family in the cephalochordate amphioxus. BMC Evol Biol 10:154.
    • (2010) BMC Evol Biol , vol.10 , pp. 154
    • Pavlicek, J.1
  • 15
    • 20444451644 scopus 로고    scopus 로고
    • A yeast polyamine acetyltransferase
    • Liu B, Sutton A, Sternglanz R (2005) A yeast polyamine acetyltransferase. J Biol Chem 280(17): 16659-16664.
    • (2005) J Biol Chem , vol.280 , Issue.17 , pp. 16659-16664
    • Liu, B.1    Sutton, A.2    Sternglanz, R.3
  • 16
    • 0025069772 scopus 로고
    • Phylogenetic distribution and function of arylalkylamine N-acetyltransferase
    • Smith TJ (1990) Phylogenetic distribution and function of arylalkylamine N-acetyltransferase. Bioessays 12(1): 30-33.
    • (1990) Bioessays , vol.12 , Issue.1 , pp. 30-33
    • Smith, T.J.1
  • 17
    • 2942709486 scopus 로고    scopus 로고
    • Evolution of cell-cell signaling in animals: Did late horizontal gene transfer from bacteria have a role?
    • Iyer LM, Aravind L, Coon SL, Klein DC, Koonin EV (2004) Evolution of cell-cell signaling in animals: Did late horizontal gene transfer from bacteria have a role? Trends Genet 20(7): 292-299.
    • (2004) Trends Genet , vol.20 , Issue.7 , pp. 292-299
    • Iyer, L.M.1    Aravind, L.2    Coon, S.L.3    Klein, D.C.4    Koonin, E.V.5
  • 18
    • 0032956319 scopus 로고    scopus 로고
    • Cellular circadian clocks in the pineal
    • Falcón J (1999) Cellular circadian clocks in the pineal. Prog Neurobiol 58(2): 121-162.
    • (1999) Prog Neurobiol , vol.58 , Issue.2 , pp. 121-162
    • Falcón, J.1
  • 19
    • 84863261062 scopus 로고    scopus 로고
    • N-acetyl serotonin derivatives as potent neuroprotectants for retinas
    • Shen J, et al. (2012) N-acetyl serotonin derivatives as potent neuroprotectants for retinas. Proc Natl Acad Sci USA 109(9): 3540-3545.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.9 , pp. 3540-3545
    • Shen, J.1
  • 20
    • 58449118344 scopus 로고    scopus 로고
    • Gnathostome phylogenomics utilizing lungfish EST sequences
    • Hallström BM, Janke A (2009) Gnathostome phylogenomics utilizing lungfish EST sequences. Mol Biol Evol 26(2): 463-471.
    • (2009) Mol Biol Evol , vol.26 , Issue.2 , pp. 463-471
    • Hallström, B.M.1    Janke, A.2
  • 21
    • 77958144056 scopus 로고    scopus 로고
    • Evolutionary origin and phylogeny of the modern holocephalans (Chondrichthyes: Chimaeriformes): A mitogenomic perspective
    • Inoue JG, et al. (2010) Evolutionary origin and phylogeny of the modern holocephalans (Chondrichthyes: Chimaeriformes): A mitogenomic perspective. Mol Biol Evol 27(11): 2576-2586.
    • (2010) Mol Biol Evol , vol.27 , Issue.11 , pp. 2576-2586
    • Inoue, J.G.1
  • 22
    • 84867577012 scopus 로고    scopus 로고
    • Functional diversity of Teleost arylalkylamine Nacetyltransferase- 2: Is the timezyme evolution driven by habitat temperature?
    • Cazaméa-Catalan D, et al. (2012) Functional diversity of Teleost arylalkylamine Nacetyltransferase- 2: Is the timezyme evolution driven by habitat temperature? Mol Ecol 21(20): 5027-5041.
    • (2012) Mol Ecol , vol.21 , Issue.20 , pp. 5027-5041
    • Cazaméa-Catalan, D.1
  • 23
    • 84877105223 scopus 로고    scopus 로고
    • Unique arylalkylamine N-acetyltransferase-2 polymorphism in salmonids and profound variations in thermal stability and catalytic efficiency conferred by two residues
    • Cazaméa-Catalan D, et al. (2013) Unique arylalkylamine N-acetyltransferase-2 polymorphism in salmonids and profound variations in thermal stability and catalytic efficiency conferred by two residues. J Exp Biol 216(Pt 10): 1938-1948.
    • (2013) J Exp Biol , vol.216 , Issue.PART 10 , pp. 1938-1948
    • Cazaméa-Catalan, D.1
  • 24
    • 0033010021 scopus 로고    scopus 로고
    • Melatonin biosynthesis: The structure of serotonin N-acetyltransferase at 2.5 A resolution suggests a catalytic mechanism
    • Hickman AB, Klein DC, Dyda F (1999) Melatonin biosynthesis: The structure of serotonin N-acetyltransferase at 2.5 A resolution suggests a catalytic mechanism. Mol Cell 3(1): 23-32.
    • (1999) Mol Cell , vol.3 , Issue.1 , pp. 23-32
    • Hickman, A.B.1    Klein, D.C.2    Dyda, F.3
  • 25
    • 0033617457 scopus 로고    scopus 로고
    • The structural basis of ordered substrate binding by serotonin N-acetyltransferase: Enzyme complex at 1.8 A resolution with a bisubstrate analog
    • Hickman AB, Namboodiri MAA, Klein DC, Dyda F (1999) The structural basis of ordered substrate binding by serotonin N-acetyltransferase: Enzyme complex at 1.8 A resolution with a bisubstrate analog. Cell 97(3): 361-369.
    • (1999) Cell , vol.97 , Issue.3 , pp. 361-369
    • Hickman, A.B.1    Namboodiri, M.A.A.2    Klein, D.C.3    Dyda, F.4
  • 26
    • 0035917466 scopus 로고    scopus 로고
    • Crystal structure of the 14-3- 3zeta:serotonin N-acetyltransferase complex. A role for scaffolding in enzyme regulation
    • Obsil T, Ghirlando R, Klein DC, Ganguly S, Dyda F (2001) Crystal structure of the 14-3- 3zeta:serotonin N-acetyltransferase complex. A role for scaffolding in enzyme regulation. Cell 105(2): 257-267.
    • (2001) Cell , vol.105 , Issue.2 , pp. 257-267
    • Obsil, T.1    Ghirlando, R.2    Klein, D.C.3    Ganguly, S.4    Dyda, F.5
  • 27
    • 79957652541 scopus 로고    scopus 로고
    • Molecular evolution of multiple arylalkylamine N-acetyltransferase (AANAT) in fish
    • Zilberman-Peled B, Bransburg-Zabary S, Klein DC, Gothilf Y (2011) Molecular evolution of multiple arylalkylamine N-acetyltransferase (AANAT) in fish. Mar Drugs 9(5): 906-921.
    • (2011) Mar Drugs , vol.9 , Issue.5 , pp. 906-921
    • Zilberman-Peled, B.1    Bransburg-Zabary, S.2    Klein, D.C.3    Gothilf, Y.4
  • 28
    • 0036299021 scopus 로고    scopus 로고
    • X-ray crystallographic studies of serotonin N-acetyltransferase catalysis and inhibition
    • Wolf E, De Angelis J, Khalil EM, Cole PA, Burley SK (2002) X-ray crystallographic studies of serotonin N-acetyltransferase catalysis and inhibition. J Mol Biol 317(2): 215-224.
    • (2002) J Mol Biol , vol.317 , Issue.2 , pp. 215-224
    • Wolf, E.1    De Angelis, J.2    Khalil, E.M.3    Cole, P.A.4    Burley, S.K.5
  • 29
    • 47249152275 scopus 로고    scopus 로고
    • Evidence that proline focuses movement of the floppy loop of arylalkylamine N-acetyltransferase (EC 2.3.1.87)
    • Pavlicek J, et al. (2008) Evidence that proline focuses movement of the floppy loop of arylalkylamine N-acetyltransferase (EC 2.3.1.87). J Biol Chem 283(21): 14552-14558.
    • (2008) J Biol Chem , vol.283 , Issue.21 , pp. 14552-14558
    • Pavlicek, J.1
  • 30
    • 0018389210 scopus 로고
    • L'organe pinéal du Brochet (Esox lucius, L.) II. Etude en microscopie électronique de la différenciation et de la rudimentation des photorécepteurs; conséquences possibles sur l'élaboration des messages sensoriels
    • Falcón J (1979) L'organe pinéal du Brochet (Esox lucius, L.) II. Etude en microscopie électronique de la différenciation et de la rudimentation des photorécepteurs; conséquences possibles sur l'élaboration des messages sensoriels. Reprod Nutr Dev 19(3A): 661-688.
    • (1979) Reprod Nutr Dev , vol.19 , Issue.3 A , pp. 661-688
    • Falcón, J.1
  • 31
    • 0019934263 scopus 로고
    • Morphology of the pineal complex of the anadromous sea lamprey, Petromyzon marinus L
    • ColeWC, Youson JH (1982) Morphology of the pineal complex of the anadromous sea lamprey, Petromyzon marinus L. Am J Anat 165(2): 131-163.
    • (1982) Am J Anat , vol.165 , Issue.2 , pp. 131-163
    • Cole, W.C.1    Youson, J.H.2
  • 32
    • 31044439837 scopus 로고    scopus 로고
    • Melatonin pathway: Breaking the 'high-at-night' rule in trout retina
    • Besseau L, et al. (2006) Melatonin pathway: Breaking the 'high-at-night' rule in trout retina. Exp Eye Res 82(4): 620-627.
    • (2006) Exp Eye Res , vol.82 , Issue.4 , pp. 620-627
    • Besseau, L.1
  • 33
    • 0036846746 scopus 로고    scopus 로고
    • The origin and evolution of model organisms
    • Hedges SB (2002) The origin and evolution of model organisms. Nat Rev Genet 3(11): 838-849.
    • (2002) Nat Rev Genet , vol.3 , Issue.11 , pp. 838-849
    • Hedges, S.B.1
  • 34
    • 33751381461 scopus 로고    scopus 로고
    • TimeTree: A public knowledge-base of divergence times among organisms
    • Hedges SB, Dudley J, Kumar S (2006) TimeTree: A public knowledge-base of divergence times among organisms. Bioinformatics 22(23): 2971-2972.
    • (2006) Bioinformatics , vol.22 , Issue.23 , pp. 2971-2972
    • Hedges, S.B.1    Dudley, J.2    Kumar, S.3
  • 35
    • 0027470424 scopus 로고
    • Melatonin secretion in vitro from the pineal complex of the lamprey Petromyzon marinus
    • Bolliet V, Ali MA, Anctil M, Zachmann A (1993) Melatonin secretion in vitro from the pineal complex of the lamprey Petromyzon marinus. Gen Comp Endocrinol 89(1): 101-106.
    • (1993) Gen Comp Endocrinol , vol.89 , Issue.1 , pp. 101-106
    • Bolliet, V.1    Ali, M.A.2    Anctil, M.3    Zachmann, A.4
  • 36
    • 0031437788 scopus 로고    scopus 로고
    • Melatonin excretion rhythms in the cultured pineal organ of the lamprey, Lampetra japonica
    • Samejima M, Tamotsu S, Uchida K, Moriguchi Y, Morita Y (1997) Melatonin excretion rhythms in the cultured pineal organ of the lamprey, Lampetra japonica. Biol Signals 6(4-6): 241-246.
    • (1997) Biol Signals , vol.6 , Issue.4-6 , pp. 241-246
    • Samejima, M.1    Tamotsu, S.2    Uchida, K.3    Moriguchi, Y.4    Morita, Y.5
  • 37
    • 0031304819 scopus 로고    scopus 로고
    • Time and time again: The phylogeny of melatonin as a transducer of biological time
    • Cassone VM, Natesan AK (1997) Time and time again: The phylogeny of melatonin as a transducer of biological time. J Biol Rhythms 12(6): 489-497.
    • (1997) J Biol Rhythms , vol.12 , Issue.6 , pp. 489-497
    • Cassone, V.M.1    Natesan, A.K.2
  • 38
    • 84864245923 scopus 로고    scopus 로고
    • Vitamin A metabolism in rod and cone visual cycles
    • Saari JC (2012) Vitamin A metabolism in rod and cone visual cycles. Annu Rev Nutr 32: 125-145.
    • (2012) Annu Rev Nutr , vol.32 , pp. 125-145
    • Saari, J.C.1
  • 39
    • 84862837301 scopus 로고    scopus 로고
    • Evolution of the genetic machinery of the visual cycle: A novelty of the vertebrate eye?
    • Albalat R (2012) Evolution of the genetic machinery of the visual cycle: A novelty of the vertebrate eye? Mol Biol Evol 29(5): 1461-1469.
    • (2012) Mol Biol Evol , vol.29 , Issue.5 , pp. 1461-1469
    • Albalat, R.1
  • 40
    • 65549145079 scopus 로고    scopus 로고
    • Night/day changes in pineal expression of >600 genes: Central role of adrenergic/cAMP signaling
    • Bailey MJ, et al. (2009) Night/day changes in pineal expression of >600 genes: Central role of adrenergic/cAMP signaling. J Biol Chem 284(12): 7606-7622.
    • (2009) J Biol Chem , vol.284 , Issue.12 , pp. 7606-7622
    • Bailey, M.J.1
  • 41
    • 84873630396 scopus 로고    scopus 로고
    • Binding of serotonin to lipid membranes
    • Peters GH, et al. (2013) Binding of serotonin to lipid membranes. J Am Chem Soc 135(6): 2164-2171.
    • (2013) J Am Chem Soc , vol.135 , Issue.6 , pp. 2164-2171
    • Peters, G.H.1
  • 42
    • 79961105328 scopus 로고    scopus 로고
    • Presence, formation and putative biological activities of Nacyl serotonins, a novel class of fatty-acid derived mediators, in the intestinal tract
    • Verhoeckx KC, et al. (2011) Presence, formation and putative biological activities of Nacyl serotonins, a novel class of fatty-acid derived mediators, in the intestinal tract. Biochim Biophys Acta 1811(10): 578-586.
    • (2011) Biochim Biophys Acta , vol.1811 , Issue.10 , pp. 578-586
    • Verhoeckx, K.C.1
  • 44
    • 0034894131 scopus 로고    scopus 로고
    • Incorporation, distribution, and metabolism of polyunsaturated fatty acids in the pineal gland of rainbow trout (Oncorhynchus mykiss) in vitro
    • Falcón J, Henderson RJ (2001) Incorporation, distribution, and metabolism of polyunsaturated fatty acids in the pineal gland of rainbow trout (Oncorhynchus mykiss) in vitro. J Pineal Res 31(2): 127-137.
    • (2001) J Pineal Res , vol.31 , Issue.2 , pp. 127-137
    • Falcón, J.1    Henderson, R.J.2
  • 45
    • 51049102167 scopus 로고    scopus 로고
    • Regulation of membrane proteins by dietary lipids: Effects of cholesterol and docosahexaenoic acid acyl chain-containing phospholipids on rhodopsin stability and function
    • Bennett MP, Mitchell DC (2008) Regulation of membrane proteins by dietary lipids: Effects of cholesterol and docosahexaenoic acid acyl chain-containing phospholipids on rhodopsin stability and function. Biophys J 95(3): 1206-1216.
    • (2008) Biophys J , vol.95 , Issue.3 , pp. 1206-1216
    • Bennett, M.P.1    Mitchell, D.C.2
  • 46
    • 33845930555 scopus 로고    scopus 로고
    • Evidence for specificity in lipid-rhodopsin interactions
    • Soubias O, Teague WE, Gawrisch K (2006) Evidence for specificity in lipid-rhodopsin interactions. J Biol Chem 281(44): 33233-33241.
    • (2006) J Biol Chem , vol.281 , Issue.44 , pp. 33233-33241
    • Soubias, O.1    Teague, W.E.2    Gawrisch, K.3
  • 47
    • 66049128566 scopus 로고    scopus 로고
    • Distinguishing among evolutionary models for the maintenance of gene duplicates
    • Hahn MW (2009) Distinguishing among evolutionary models for the maintenance of gene duplicates. J Hered 100(5): 605-617.
    • (2009) J Hered , vol.100 , Issue.5 , pp. 605-617
    • Hahn, M.W.1
  • 48
    • 84872239507 scopus 로고    scopus 로고
    • Duplication and diversification of the spermidine/spermine N1-acetyltransferase 1 genes in zebrafish
    • Lien YC, Ou TY, Lin YT, Kuo PC, Lin HJ (2013) Duplication and diversification of the spermidine/spermine N1-acetyltransferase 1 genes in zebrafish. PLoS One 8(1):e54017.
    • (2013) PLoS One , vol.8 , Issue.1
    • Lien, Y.C.1    Ou, T.Y.2    Lin, Y.T.3    Kuo, P.C.4    Lin, H.J.5
  • 51
    • 33646695203 scopus 로고    scopus 로고
    • Evolution of arylalkylamine N-acetyltransferase: Emergence and divergence
    • Coon SL, Klein DC (2006) Evolution of arylalkylamine N-acetyltransferase: Emergence and divergence. Mol Cell Endocrinol 252(1-2): 2-10.
    • (2006) Mol Cell Endocrinol , vol.252 , Issue.1-2 , pp. 2-10
    • Coon, S.L.1    Klein, D.C.2


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