Approaches to Determine Protein Ubiquitination Residue Types.
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 non-lysine 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.
['Chen|Qian|Q|', 'Yang|Xiaoyuan|X|', 'Xie|Qi|Q|']
D000595:Amino Acid Sequence D003545:Cysteine D008715:Methionine D008967:Molecular Biology D011499:Protein Processing, Post-Translational D011506:Proteins D012694:Serine D025801:Ubiquitin D054875:Ubiquitination
Ubiquitination Posttranslational modification Serine/threonine Cysteine Hydrolysis