Yng1 PHD Finger Binding to H3 Trimethylated at K4 Promotes NuA3 HAT Activity at K14 of H3 and Transcription at a Subset of Targeted ORFs
Open Access
- 8 December 2006
- journal article
- Published by Elsevier in Molecular Cell
- Vol. 24 (5) , 785-796
- https://doi.org/10.1016/j.molcel.2006.10.026
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- The Yng1p Plant Homeodomain Finger Is a Methyl-Histone Binding Module That Recognizes Lysine 4-Methylated Histone H3Molecular and Cellular Biology, 2006
- Reading protein modifications with interaction domainsNature Reviews Molecular Cell Biology, 2006
- ING2 PHD domain links histone H3 lysine 4 methylation to active gene repressionNature, 2006
- Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2Nature, 2006
- Methylation of Histone H3 Mediates the Association of the NuA3 Histone Acetyltransferase with ChromatinMolecular and Cellular Biology, 2006
- A Bivalent Chromatin Structure Marks Key Developmental Genes in Embryonic Stem CellsCell, 2006
- Dynamic Acetylation of All Lysine 4–Methylated Histone H3 in the Mouse Nucleus: Analysis at c-fos and c-junPLoS Biology, 2005
- Translating the Histone CodeScience, 2001
- Genome-Wide Location and Function of DNA Binding ProteinsScience, 2000
- The language of covalent histone modificationsNature, 2000