title: Synthesis of atypical diubiquitin chains.
abstract: Post-translational modification of proteins with ubiquitin (Ub) and Ub chains controls numerous biochemical events. Although it has been proven that all Ub-Ub linkages are formed in cells, studies have been limited for a long time to K48 and K63 chains as these can be generated biochemically. Access to the remaining (atypical) Ub-Ub chain types has been hampered by a lack of specific E2 enzymes. In this chapter we present a solution to this problem by using a native chemical ligation approach to obtain all other (i.e. K6, K11, K27, K29 and K33) diubiquitin chains.
authors.affiliation: Division of Cell Biology, Netherlands Cancer Institute, Amsterdam, The Netherlands.
authors.forename: Farid El
authors.initials: FE
authors.lastname: Oualid
authors.forename: Dharjath S
authors.initials: DS
authors.lastname: Hameed
authors.forename: Dris El
authors.initials: DE
authors.lastname: Atmioui
authors.forename: Henk
authors.initials: H
authors.lastname: Hilkmann
authors.forename: Huib
authors.initials: H
authors.lastname: Ovaa
mesh_terms: D025821:Polyubiquitin / Q000138:chemical synthesis* / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D054875:Ubiquitination; D014452:Ubiquitins / Q000138:chemical synthesis
chemical_list: D014452:Ubiquitins; C075986:diubiquitin conjugate; D025821:Polyubiquitin