Monoubiquitination of histone H2B is intrinsic to the Bre1 RING domain-Rad6 interaction and augmented by a second Rad6-binding site on Bre1.
Turco, Eleonora; Gallego, Laura D; Schneider, Maren; Köhler, Alwin.
J Biol Chem
; 290(9): 5298-310, 2015 Feb 27.
Artigo em Inglês | MEDLINE | ID: mdl-25548288
Role of a non-canonical surface of Rad6 in ubiquitin conjugating activity.
Sequential Poly-ubiquitylation by Specialized Conjugating Enzymes Expands the Versatility of a Quality Control Ubiquitin Ligase.
A nuclear ubiquitin-proteasome pathway targets the inner nuclear membrane protein Asi2 for degradation.
Rad6-Bre1-mediated H2B ubiquitination regulates telomere replication by promoting telomere-end resection.
Phase separation directs ubiquitination of gene-body nucleosomes.
UBC9 Mutant Reveals the Impact of Protein Dynamics on Substrate Selectivity and SUMO Chain Linkages.
The Histone Modification Domain of Paf1 Complex Subunit Rtf1 Directly Stimulates H2B Ubiquitylation through an Interaction with Rad6.
Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C.
Types of Ubiquitin Ligases.
The CUE Domain of Cue1 Aligns Growing Ubiquitin Chains with Ubc7 for Rapid Elongation.