Ontology highlight
ABSTRACT:
SUBMITTER: Gallego LD
PROVIDER: S-EPMC5035881 | biostudies-literature | 2016 Sep
REPOSITORIES: biostudies-literature
Gallego Laura D LD Ghodgaonkar Steger Medini M Polyansky Anton A AA Schubert Tobias T Zagrovic Bojan B Zheng Ning N Clausen Tim T Herzog Franz F Köhler Alwin A
Proceedings of the National Academy of Sciences of the United States of America 20160906 38
Cotranscriptional ubiquitination of histone H2B is key to gene regulation. The yeast E3 ubiquitin ligase Bre1 (human RNF20/40) pairs with the E2 ubiquitin conjugating enzyme Rad6 to monoubiquitinate H2B at Lys123. How this single lysine residue on the nucleosome core particle (NCP) is targeted by the Rad6-Bre1 machinery is unknown. Using chemical cross-linking and mass spectrometry, we identified the functional interfaces of Rad6, Bre1, and NCPs in a defined in vitro system. The Bre1 RING domain ...[more]