Monoubiquitination of Histone H2B Is Intrinsic to the Bre1 RING Domain-Rad6 Interaction and Augmented by a Second Rad6-binding Site on Bre1
Open Access
- 1 February 2015
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 290 (9) , 5298-5310
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Role of histone H2A ubiquitination in Polycomb silencingNature, 2004
- A Conserved RING Finger Protein Required for Histone H2B Monoubiquitination and Cell Size ControlMolecular Cell, 2003
- Bre1, an E3 Ubiquitin Ligase Required for Recruitment and Substrate Selection of Rad6 at a PromoterMolecular Cell, 2003
- Two RING finger proteins mediate cooperation between ubiquitin‐conjugating enzymes in DNA repairThe EMBO Journal, 2000
- Rad6-Dependent Ubiquitination of Histone H2B in YeastScience, 2000
- The E2–E3 interaction in the N‐end rule pathway: the RING‐H2 finger of E3 is required for the synthesis of multiubiquitin chainThe EMBO Journal, 1999
- Crystal structure of the nucleosome core particle at 2.8 Å resolutionNature, 1997
- Characterization of nucleosome core particles containing histone proteins made in bacteria 1 1Edited by A. KlugJournal of Molecular Biology, 1997
- Domains Required for Dimerization of Yeast Rad6 Ubiquitin-Conjugating Enzyme and Rad18 DNA Binding ProteinMolecular and Cellular Biology, 1997
- The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzymeNature, 1987