The mechanism of cross-talk between histone H2B ubiquitination and H3 methylation by Dot1L
Explore this paper's citation graph
Summary
This study provides a comprehensive mechanism of cross-talk between histone ubiquitination and methylation and reveals an unexpected structural plasticity in histones that makes it possible for histone-modifying enzymes to access residues within the nucleosome core.
- Type
- preprint
- Published
- 2018-12-19
- Cited by
- 0
- References
- 67
- Access
- Open access
- OpenAlex
- https://openalex.org/W2905256649
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:92603584
Keywords
Histone H3, Histone octamer, Nucleosome, Histone methyltransferase, Histone methylation
References
- The Nucleosomal Surface as a Docking Station for Kaposi's Sarcoma Herpesvirus LANA
- Reconstitution of nucleosome core particles from recombinant histones and DNA.
- Preparation of nucleosome core particle from recombinant histones.
- Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
- A charge-based interaction between histone H4 and Dot1 is required for H3K79 methylation and telomere silencing: identification of a new trans-histone pathway.
- H3K79 methylation profiles define murine and human MLL-AF4 leukemias
- Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain.
- Structure activity analysis of semisynthetic nucleosomes: Mechanistic insights into the stimulation of Dot1L by ubiquitylated histone H2B
- Efficient incorporation of unsaturated methionine analogues into proteins in vivo
- New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning.
- Ubiquitination of Histone H2B by Rad6 Is Required for Efficient Dot1-mediated Methylation of Histone H3 Lysine 79*
- Dot1 and Histone H3K79 Methylation in Natural Telomeric and HM Silencing
- Catalytic site remodelling of the DOT1L methyltransferase by selective inhibitors
- Histone H2B ubiquitin ligase RNF20 is required for MLL-rearranged leukemia
- Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation
- Structure of RCC1 chromatin factor bound to the nucleosome core particle
- Degree of Recruitment of DOT1L to MLL-AF9 Defines Level of H3K79 Di- and Tri-methylation on Target Genes and Transformation Potential
- Gene silencing: Trans-histone regulatory pathway in chromatin
- Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks
- Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation.
Cited by
No citing papers recorded for this paper.
Related papers
- Points of contact between histone H1 and the histone octamer.
- Histone H4 lysine 91 acetylation a core domain modification associated with chromatin assembly.
- Effects of Sin− versions of histone H4 on yeast chromatin structure and function
- Histone-like transcription factors in eukaryotes.
- In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays.
- Expression and purification of recombinant histones and nucleosome reconstitution.
- Histone variants: key players of chromatin
- Small region of Rtf1 protein can substitute for complete Paf1 complex in facilitating global histone H2B ubiquitylation in yeast