Structural mechanism for the recognition and ubiquitination of a single nucleosome residue by Rad6-Bre1.
Gallego, Laura D; Ghodgaonkar Steger, Medini; Polyansky, Anton A; Schubert, Tobias; Zagrovic, Bojan; Zheng, Ning; Clausen, Tim; Herzog, Franz; Köhler, Alwin.
Proc Natl Acad Sci U S A
; 113(38): 10553-8, 2016 09 20.
Artigo em Inglês | MEDLINE | ID: mdl-27601672
Phase separation directs ubiquitination of gene-body nucleosomes.
Monoubiquitination of histone H2B is intrinsic to the Bre1 RING domain-Rad6 interaction and augmented by a second Rad6-binding site on Bre1.
Role of a non-canonical surface of Rad6 in ubiquitin conjugating activity.
The mechanism of linkage-specific ubiquitin chain elongation by a single-subunit E2.
Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis.
Crystal structure of a human ubiquitin E1-ubiquitin complex reveals conserved functional elements essential for activity.
The mechanism of OTUB1-mediated inhibition of ubiquitination.
Synergistic recruitment of UbcH7~Ub and phosphorylated Ubl domain triggers parkin activation.
Mechanism of Cross-talk between H2B Ubiquitination and H3 Methylation by Dot1L.
Insights into ubiquitin transfer cascades from a structure of a UbcH5B approximately ubiquitin-HECT(NEDD4L) complex.