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摘要:Selenoprotein expression using Escherichia coli system redefines specific UGA codon from translational termination to selenocysteine(Sec) insertion.Previously,we found that a predefine UGG codon was redirected for Sec incorporation into recombinant selenoprotein,using efficient wobble decoding mediated by E.coli selenoprotein insertion machinery.In this study,wc indirectly examined the efficiency of Sec insertion through the production of enzymatically active TrxRl,using single point-mutation at Sec-specfic tRNA in place of the native tRNASec,with or without the SECIS element.Based upon new observations,we illuminated some criteria when the selenoprotein translation machinery mediates UGG-mediated wobble decoding for Sec incorporation.Clearly,a function bacterial-type SECIS element was required for selenoprotein production.Some key nucloclidc sites of tRNASec were essential for selenoprotein synthesis and to increase the Sec insertion efficiency.This study reveal an unknown flexibility in E.coli tRNASec that may be of importance for an in-depth understanding of the bacterial Sec insertion mechanisms.
会议名称:

全球华人生物学家大会暨第十六届美洲华人生物科学学会学术研讨会

会议时间:

2017-06-29

会议地点:

中国浙江杭州

  • 专辑:

    基础科学

  • 专题:

    生物学; 生物学

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    Q75

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