ZhaoBoyleDuvalEtAl2009

Référence

Zhao, N., Boyle, B., Duval, I., Ferrer, J.L., Lin, H., Seguin, A., MacKay, J., Chen, F. (2009) SABATH methyltransferases from white spruce (Picea glauca): gene cloning, functional characterization and structural analysis. Tree Physiology, 29(7):947-957.

Résumé

Known members of the plant SABATH family of methyltransferases have important biological functions by methylating hormones, signalling molecules and other metabolites. While all previously characterized SABATH genes were isolated from angiosperms, in this article, we report on the isolation and functional characterization of SABATH genes from white spruce (Picea glauca [Moench] Voss), a gymnosperm. Through EST database search, three genes that encode proteins significantly homologous to known SABATH proteins were identified from white spruce. They were named PgSABATH1, PgSABATH2 and PgSABATH3, respectively. Full length cDNAs of these three genes were cloned and expressed in Escherichia coli. The E. coli-expressed recombinant proteins were tested for methyltransferase activity with a large number of compounds. While no activity was detected for PgSABATH2 and PgSABATH3, PgSABATH1 displayed the highest level of catalytic activity with indole-3-acetic acid (IAA). PgSABATH1 was, therefore, renamed PgIAMT1. Under steady-state conditions, PgIAMT1 exhibited apparent K-m values of 18.2M for IAA. Homology-based structural modelling of PgIAMT1 revealed that the active site of PgIAMT1 is highly similar to other characterized IAMTs from angiosperms. PgIAMT1 showed expression in multiple tissues, with the highest level of expression detected in embryonic tissues. During somatic embryo maturation, a significant reduction in PgIAMT1 transcript levels was observed when developing cotyledons become apparent which is indicative of mature embryos. The biological roles of white spruce SABATH genes, especially those of PgIAMT1, and the evolution of the SABATH family are discussed.

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@ARTICLE { ZhaoBoyleDuvalEtAl2009,
    AUTHOR = { Zhao, N. and Boyle, B. and Duval, I. and Ferrer, J.L. and Lin, H. and Seguin, A. and MacKay, J. and Chen, F. },
    TITLE = { SABATH methyltransferases from white spruce (Picea glauca): gene cloning, functional characterization and structural analysis },
    JOURNAL = { Tree Physiology },
    YEAR = { 2009 },
    VOLUME = { 29 },
    PAGES = { 947-957 },
    NUMBER = { 7 },
    MONTH = { jul },
    AF = { Zhao, NanEOLEOLBoyle, BrianEOLEOLDuval, IsabelleEOLEOLFerrer, Jean-LucEOLEOLLin, HongEOLEOLSeguin, ArmandEOLEOLMackay, JohnEOLEOLChen, Feng },
    C1 = { [Zhao, Nan; Chen, Feng] Univ Tennessee, Dept Plant Sci, Knoxville, TN 37996 USA.EOLEOL[Boyle, Brian; Mackay, John] Univ Laval, Ctr Etud Foret, Quebec City, PQ G1V 0A6, Canada.EOLEOL[Duval, Isabelle; Seguin, Armand] Nat Resources Canada, Canadian Forest Serv, Quebec City, PQ G1V 4C7, Canada.EOLEOL[Ferrer, Jean-Luc] Univ Grenoble 1, Inst Biol Struct, CEA, CNRS, F-38027 Grenoble 1, France.EOLEOL[Lin, Hong] USDA ARS, Parlier, CA 93648 USA. },
    DE = { gene expression; high-throughput enzyme assay; indole-3-acetic acid;EOLEOLsomatic embryogenesis },
    DI = { 10.1093/treephys/tpp023 },
    EM = { fengc@utk.edu },
    FU = { University of Tennessee ; genome Canada and genome Quebec },
    FX = { This work was partly supported by startup research funds from theEOLEOLUniversity of Tennessee (to F. C.) and genome Canada and genome QuebecEOLEOLgrants for the Arborea project (to A. S. and J.M.). The authors wouldEOLEOLlike to thank C. Levasseur, C. Jones and K. Klimaszewska from theEOLEOLCanadian Forest Service for the help with embryonal tissue culture andEOLEOLF. Bedon and C. Bomal for sharing stressed P. glauca material. },
    GA = { 460YC },
    J9 = { TREE PHYSIOL },
    JI = { Tree Physiol. },
    LA = { English },
    NR = { 41 },
    PA = { GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND },
    PG = { 11 },
    PI = { OXFORD },
    RP = { Chen, F, Univ Tennessee, Dept Plant Sci, Knoxville, TN 37996 USA. },
    SC = { Forestry },
    SN = { 0829-318X },
    TC = { 0 },
    UT = { ISI:000267227900010 },
    ABSTRACT = { Known members of the plant SABATH family of methyltransferases have important biological functions by methylating hormones, signalling molecules and other metabolites. While all previously characterized SABATH genes were isolated from angiosperms, in this article, we report on the isolation and functional characterization of SABATH genes from white spruce (Picea glauca [Moench] Voss), a gymnosperm. Through EST database search, three genes that encode proteins significantly homologous to known SABATH proteins were identified from white spruce. They were named PgSABATH1, PgSABATH2 and PgSABATH3, respectively. Full length cDNAs of these three genes were cloned and expressed in Escherichia coli. The E. coli-expressed recombinant proteins were tested for methyltransferase activity with a large number of compounds. While no activity was detected for PgSABATH2 and PgSABATH3, PgSABATH1 displayed the highest level of catalytic activity with indole-3-acetic acid (IAA). PgSABATH1 was, therefore, renamed PgIAMT1. Under steady-state conditions, PgIAMT1 exhibited apparent K-m values of 18.2M for IAA. Homology-based structural modelling of PgIAMT1 revealed that the active site of PgIAMT1 is highly similar to other characterized IAMTs from angiosperms. PgIAMT1 showed expression in multiple tissues, with the highest level of expression detected in embryonic tissues. During somatic embryo maturation, a significant reduction in PgIAMT1 transcript levels was observed when developing cotyledons become apparent which is indicative of mature embryos. The biological roles of white spruce SABATH genes, especially those of PgIAMT1, and the evolution of the SABATH family are discussed. },
    KEYWORDS = { ACID CARBOXYL METHYLTRANSFERASE; CAFFEINE SYNTHASE GENE; ADENOSYL-L-METHIONINE; ARABIDOPSIS-THALIANA; SOMATIC EMBRYOS; INDOLE-3-ACETIC-ACID METHYLTRANSFERASE; WOOD FORMATION; PLANT-GROWTH; HYBRID ASPEN; BIOSYNTHESIS },
    OWNER = { sobru1 },
    PUBLISHER = { Oxford Univ Press },
    TIMESTAMP = { 2009.07.06 },
}

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