Characterization of HIV Tat modifications using novel methyl-lysine-specific antibodies |
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| Authors: | Sara Pagans Naoki Sakane Martina Schnölzer Melanie Ott |
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| Affiliation: | 1. Gladstone Institute of Virology and Immunology, University of California, San Francisco, CA 94158, USA;2. Pharmaceutical Frontier Research Laboratory, Japan Tobacco, 1-13-2 Fukuura, Kanazawa-ku, Yokohama, Kanagawa 236-0004, Japan;3. Functional Proteome Analysis, German Cancer Research Center (DKFZ), 69120 Heidelberg, Germany;4. Department of Medicine, University of California, San Francisco, CA 94110, USA |
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| Abstract: | Modification-specific antibodies are important tools to examine the dynamics and functions of posttranslational protein modifications in cells. Here, we describe in detail the generation of polyclonal antibodies specific for mono-, di-, and trimethylated lysine 51 within the HIV transactivator Tat. Lysine 51 is a highly conserved residue located in the RNA-binding region of Tat and the target of lysine methyltransferases KMT1E (SETDB1) and KMT7 (Set7/9). Using affinity-purified methyl-specific antibodies of Tat, we find that cellular Tat is predominantly monomethylated at lysine 51, a modification enhanced by coexpression of KMT7. |
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