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Nonenzymatic Ubiquitylation

Authors

  • Dr. Tomasz Fekner,

    1. Department of Chemistry, Department of Biochemistry and the Ohio State Biophysics Program, The Ohio State University, 484 W 12th Avenue, Columbus, OH 43210 (USA), Fax: (+1) 614-292-6773
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  • Xin Li,

    1. Department of Chemistry, Department of Biochemistry and the Ohio State Biophysics Program, The Ohio State University, 484 W 12th Avenue, Columbus, OH 43210 (USA), Fax: (+1) 614-292-6773
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  • Prof. Michael K. Chan

    Corresponding author
    1. Department of Chemistry, Department of Biochemistry and the Ohio State Biophysics Program, The Ohio State University, 484 W 12th Avenue, Columbus, OH 43210 (USA), Fax: (+1) 614-292-6773
    • Department of Chemistry, Department of Biochemistry and the Ohio State Biophysics Program, The Ohio State University, 484 W 12th Avenue, Columbus, OH 43210 (USA), Fax: (+1) 614-292-6773
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Abstract

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Enzymes need not apply: Recently developed synthetic methods make it possible to site-specifically modify proteins with ubiquitin by chemical means, thus providing an attractive alternative to laborious protocols relying on the identification and isolation of cognate ligases. Some of these methods, especially if introducing a mutation point into a target can be tolerated, are sufficiently straightforward for routine use.

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