Chemical methods for protein site-specific ubiquitination

Convergent chemical synthesis of histone H2B protein for the site-specific ubiquitination at Lys34.

Site-specific chemical modification procedures.

DNA-binding regulates site-specific ubiquitination of IRF-1.

Understanding the determinants for site-specific ubiquitination by E3 ligase components of the ubiquitin machinery is proving to be a challenge. In the present study we investigate the role of an E3 ligase docking site (Mf2 domain) in an intrinsically disordered domain of IRF-1 [IFN (interferon) regulatory factor-1], a short-lived IFNγ-regulated transcription factor, in ubiquitination of the pr...

Site-Specific Phosphorylation of IκBα by a Novel Ubiquitination-Dependent Protein Kinase Activity

Recently, it has been shown that signal-induced degradation of I␬B␣ is mediated by the ubiquitin (Ub)– *ProScript, Incorporated proteasome pathway (Chen et al., 1995; Scherer et al., 38 Sidney Street 1995; Alkalay et al., 1995b). In this pathway, a protein Cambridge, Massachusetts 02139 targeted for degradation is first modified by covalent † Harvard University attachment of Ub, a highly conser...

Traceless and Site-Specific Ubiquitination of Recombinant Proteins

Protein ubiquitination is a post-translational modification that regulates almost all aspects of eukaryotic biology. Here we discover the first routes for the efficient site-specific incorporation of δ-thiol-L-lysine (7) and δ-hydroxy-L-lysine (8) into recombinant proteins, via evolution of a pyrrolysyl-tRNA synthetase/tRNA(CUA) pair. We combine the genetically directed incorporation of 7 with ...