Protein Arginine Allylation and Subsequent Fluorophore Targeting

Authors

  • Yixin Zhang,

    1. Division of Biotechnology, Dalian Institute of Chemical Physics, 116023 Dalian (China)
    2. University of Chinese Academy of Sciences, 19A Yuquanlu, 100049 Beijing (China)
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  • Yanbo Pan,

    1. Key Laboratory of Separation Sciences for Analytical Chemistry, Dalian Institute of Chemical Physics, 116023 Dalian (China)
    2. University of Chinese Academy of Sciences, 19A Yuquanlu, 100049 Beijing (China)
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  • Dr. Wei Yang,

    1. Division of Biotechnology, Dalian Institute of Chemical Physics, 116023 Dalian (China)
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  • Wujun Liu,

    1. Division of Biotechnology, Dalian Institute of Chemical Physics, 116023 Dalian (China)
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  • Prof. Dr. Hanfa Zou,

    1. Key Laboratory of Separation Sciences for Analytical Chemistry, Dalian Institute of Chemical Physics, 116023 Dalian (China)
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  • Prof. Dr. Zongbao K. Zhao

    Corresponding author
    1. Division of Biotechnology, Dalian Institute of Chemical Physics, 116023 Dalian (China)
    • Division of Biotechnology, Dalian Institute of Chemical Physics, 116023 Dalian (China)
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Abstract

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Protein allylation and fluorophore targeting: Arginine residues of the yeast nuclear ribonucleoprotein Npl3 were extensively modified by Hmt1-catalyzed allylation reaction with allyl-SAM as the allyl group donor. The allylated protein was further treated with tetrazole compounds under UV irradiation, leading to formation of protein-attached fluorescent products.

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