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A Genetically Encoded 19F NMR Probe for Tyrosine Phosphorylation

Authors

  • Fahui Li,

    1. Laboratory of Non-coding RNA, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing, 100101 (China)
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    • These authors contributed equally to this work.

  • Pan Shi,

    1. School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026 (China)
    2. High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, Anhui, 230031 (China)
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    • These authors contributed equally to this work.

  • Jiasong Li,

    1. School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026 (China)
    2. Laboratory of Non-coding RNA, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing, 100101 (China)
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    • These authors contributed equally to this work.

  • Fan Yang,

    1. Department of Physiology, Shandong University School of Medicine, Jinan 250012 (China)
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  • Tianyuan Wang,

    1. Laboratory of Non-coding RNA, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing, 100101 (China)
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  • Wei Zhang,

    1. Laboratory of Non-coding RNA, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing, 100101 (China)
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  • Feng Gao,

    1. Laboratory of Non-coding RNA, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing, 100101 (China)
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  • Wei Ding,

    1. Laboratory of Non-coding RNA, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing, 100101 (China)
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  • Dong Li,

    1. School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026 (China)
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  • Juan Li,

    1. School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026 (China)
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  • Ying Xiong,

    1. School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026 (China)
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  • Jinpeng Sun,

    1. Department of Physiology, Shandong University School of Medicine, Jinan 250012 (China)
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  • Weimin Gong,

    Corresponding author
    1. Laboratory of Non-coding RNA, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing, 100101 (China)
    • Laboratory of Non-coding RNA, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing, 100101 (China)
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  • Changlin Tian,

    Corresponding author
    1. School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026 (China)
    2. High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, Anhui, 230031 (China)
    • School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026 (China)
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  • Jiangyun Wang

    Corresponding author
    1. Laboratory of Non-coding RNA, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing, 100101 (China)
    • Laboratory of Non-coding RNA, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing, 100101 (China)
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  • We gratefully acknowledge the Major State Basic Research Program of China (grant numbers 2010CB912301 and 2009CB825505), the National Science Foundation of China (grant numbers 90913022, 31000364, 31170817, and 31100563), the CAS grant (grant number KSCX2-EW-G-7) to J.W., F.L., C.T., and Y.X. We thank Professors Zongchao Jia and Jingxuan Pan for helpful discussion.

Abstract

original image

Simple and selective: Tyrosine phosphorylation is a pivotal post-translational modification which regulates the enzymatic activity, protein conformation, and protein–protein interactions. The highly efficient genetic incorporation of 3,5-difluorotyrosine (F2Y) in E. coli and the use of F2Y as a 19F NMR probe for the tyrosine phosphorylation are reported (see picture).

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