title: Synthesis and analysis of K11-linked ubiquitin chains.
abstract: Much has been learned about protein ubiquitination by studying the structural, biochemical, and biophysical properties of ubiquitin chains in vitro. However, these analyses were limited to K48-, K63-linked, and linear ubiquitin chains. Only recently, enzymatic and chemical assembly systems for the remaining chain types have been developed. Here, we describe a method to synthesise K11-linked ubiquitin chains in vitro by exploiting the intrinsic K11-specificity of the E2 enzyme UBE2S.
authors.affiliation: Protein and Nucleic Acid Chemistry Division, MRC Laboratory of Molecular Biology, Cambridge, UK.
authors.forename: Anja
authors.initials: A
authors.lastname: Bremm
authors.forename: David
authors.initials: D
authors.lastname: Komander
mesh_terms: D003001:Cloning, Molecular / Q000379:methods; D006801:Humans; D025821:Polyubiquitin / Q000138:chemical synthesis* / Q000737:chemistry; D011993:Recombinant Fusion Proteins / Q000235:genetics; D013379:Substrate Specificity; D044763:Ubiquitin-Conjugating Enzymes / Q000235:genetics / Q000378:metabolism*; D054875:Ubiquitination
chemical_list: D011993:Recombinant Fusion Proteins; D025821:Polyubiquitin; C544962:Ube2S protein, human; D044763:Ubiquitin-Conjugating Enzymes