Ubiquitylation � the attachment of ubiquitin to a protein � is a widely utilized posttranslational modification in eukarytes and is involved in various aspects of cellular function. Three distinct enzymes, known as the E1-E3 system, collaborate to achieve a site-specific tagging of ubiquitin to a protein target. The majority of the studies in the field rely on the in vitro enzymatic reconstitution of this complex modification for the protein of interest. This process is often challenged by the heterogeneity of the modified protein, the isolation of the specific ligase, and obtaining reasonable quantities of the ubiquitylated protein. In this talk, I will present our recent development on the highly efficient peptide and protein ubiquitylation. The chemical synthesis of homogeneous ubiquitylated alpha-synuclein to study the effect of ubiquitylation in Parkinson's disease will be presented. Moreover, the use of our chemical tools in the chemical synthesis of the polyubiquitin chain will also be discussed.

Advanced chemical tools to study ubiquitin biology

241st National Meeting (2011)

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