Ubiquitination is an important posttranslational modification in eukaryotic organisms and plays a central role in many signaling pathways in plants. Most ubiquitination typically occurs on substrate lysine residues, forming a covalent isopeptide bond. Some recent reports suggested ubiquitin can be attached to nonlysine sites such as serine/threonine, cysteine or the N-terminal methionine, via oxyester or thioester linkages, respectively. In the present protocol, we developed a convenient in vitro assay for investigating ubiquitination on Ser/Thr and Cys residues.
CITATION STYLE
Chen, Q., Yang, X., & Xie, Q. (2016). Approaches to determine protein ubiquitination residue types. In Methods in Molecular Biology (Vol. 1450, pp. 3–10). Humana Press Inc. https://doi.org/10.1007/978-1-4939-3759-2_1
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