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The Taf14 YEATS domain is a reader of histone crotonylation
TLDR
The YEATS domain is reported as an effective reader of histone lysine crotonylation – an epigenetic signature associated with active transcription that engages crotonyllysine via a unique π-π-π Stacking mechanism and that other YEAT domains have crotonytysine binding activity. Expand
A non-active-site SET domain surface crucial for the interaction of MLL1 and the RbBP5/Ash2L heterodimer within MLL family core complexes.
TLDR
Results suggest that amino acids from this surface, which is termed the Kabuki interaction surface or KIS, are required for formation of a second active site within SET1 family core complexes. Expand
Biochemical Reconstitution and Phylogenetic Comparison of Human SET1 Family Core Complexes Involved in Histone Methylation*
TLDR
This investigation reconstituted each human SET1 family core complex and compared subunit assembly and enzymatic activities, finding that in the absence of WRAD, all but one SET domain catalyzes at least weak H3K4 monomethylation. Expand
Histone deacetylase 10 structure and molecular function as a polyamine deacetylase
TLDR
This work sets a foundation for studying the chemical biology of autophagy through the structure-based design of inhibitors that may also serve as new leads for cancer chemotherapy. Expand
Structure/Function Analysis of Recurrent Mutations in SETD2 Protein Reveals a Critical and Conserved Role for a SET Domain Residue in Maintaining Protein Stability and Histone H3 Lys-36
TLDR
Data imply a critical role for Arg-1625 in maintaining the protein interaction with H3 and specific H3K36me3 function of this enzyme, which is conserved from yeast to humans, and may provide a refined biochemical explanation for how H 3K 36me3 loss leads to genomic instability and cancer. Expand
Targeted Disruption of the Interaction between WD-40 Repeat Protein 5 (WDR5) and Mixed Lineage Leukemia (MLL)/SET1 Family Proteins Specifically Inhibits MLL1 and SETd1A Methyltransferase Complexes*
TLDR
A peptidomimetic is designed that binds WDR5 (Kd ∼3 nm) and selectively inhibits activity of MLL1 and SETd1A core complexes within the SET1 family, revealing thatSET1 family complexes with the weakest Win motif-WDR5 interaction are more susceptible to Win motif -based inhibitors. Expand
Histone peptide microarray screen of chromo and Tudor domains defines new histone lysine methylation interactions
TLDR
A high-throughput histone peptide microarray platform is used to interrogate 83 known and putative histone reader domains from the chromo and Tudor domain families to identify their interactions and characterize the influence of neighboring PTMs on these interactions. Expand
Recognition of Histone Crotonylation by Taf14 Links Metabolic State to Gene Expression.
TLDR
These findings expose an unexpected link between metabolic flux and transcription and demonstrate that histone crotonylation and Taf14 participate in the repression of energy-demanding gene expression. Expand
Unique Role of the WD-40 Repeat Protein 5 (WDR5) Subunit within the Mixed Lineage Leukemia 3 (MLL3) Histone Methyltransferase Complex*
TLDR
A unique role for WDR5 is demonstrated in modulating the enzymatic activity of the MLL3 core complex, where unlike MLL1, the M LL3 SET domain assembles with the RbBP5/Ash2L heterodimer independently of the Win motif-WDR5 interaction. Expand
Automethylation Activities within the Mixed Lineage Leukemia-1 (MLL1) Core Complex Reveal Evidence Supporting a “Two-active Site” Model for Multiple Histone H3 Lysine 4 Methylation*
TLDR
The suppressor of variegation, enhancer of zeste, trithorax (SET) domains from human MLL1 and Drosophila Tritorax undergo robust intramolecular automethylation reactions at an evolutionarily conserved cysteine residue in the active site, which is inhibited by unmodified histone H3. Expand
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