title: Inhibiting the protein ubiquitination cascade by ubiquitin-mimicking short peptides.
abstract: Short heptapeptides were identified to function as ubiquitin (UB) mimics that are activated by E1 and form thioester conjugates with E1, E2, and HECT type E3 enzymes. The activities (k(cat)/K(1/2)) of E1 with the UB-mimicking peptides are 130-1,400-fold higher than the equally long peptide with the native C-terminal sequence of UB. By forming covalent conjugates with E1, E2, and E3 enzymes, the UB-mimicking peptides can block the transfer of native UB through the cascade.
authors.affiliation: Department of Chemistry, University of Chicago, Chicago, Illinois 60637, USA.
authors.forename: Bo
authors.initials: B
authors.lastname: Zhao
authors.forename: Chan Hee J
authors.initials: CH
authors.lastname: Choi
authors.forename: Karan
authors.initials: K
authors.lastname: Bhuripanyo
authors.forename: Eric B
authors.initials: EB
authors.lastname: Villhauer
authors.forename: Keya
authors.initials: K
authors.lastname: Zhang
authors.forename: Hermann
authors.initials: H
authors.lastname: Schindelin
authors.forename: Jun
authors.initials: J
authors.lastname: Yin
mesh_terms: D015394:Molecular Structure; D010455:Peptides / Q000378:metabolism*; D025801:Ubiquitin / Q000378:metabolism*; D044763:Ubiquitin-Conjugating Enzymes / Q000378:metabolism*; D054875:Ubiquitination / Q000187:drug effects*
chemical_list: D010455:Peptides; D025801:Ubiquitin; D044763:Ubiquitin-Conjugating Enzymes