Double chromodomains cooperate to recognize the methylated histone H3 tail
Top Cited Papers
- 22 December 2005
- journal article
- research article
- Published by Springer Science and Business Media LLC in Nature
- Vol. 438 (7071), 1181-1185
- https://doi.org/10.1038/nature04290
Abstract
Chromodomains are modules implicated in the recognition of lysine-methylated histone tails and nucleic acids1,2. CHD (for chromo-ATPase/helicase-DNA-binding) proteins regulate ATP-dependent nucleosome assembly and mobilization through their conserved double chromodomains and SWI2/SNF2 helicase/ATPase domain3,4,5. The Drosophila CHD1 localizes to the interb ands and puffs of the polytene chromosomes, which are classic sites of transcriptional activity6. Other CHD isoforms (CHD3/4 or Mi-2) are important for nucleosome remodelling in histone deacetylase complexes7,8. Deletion of chromodomains impairs nucleosome binding and remodelling by CHD proteins4. Here we describe the structure of the tandem arrangement of the human CHD1 chromodomains, and its interactions with histone tails. Unlike HP1 and Polycomb proteins that use single chromodomains to bind to their respective methylated histone H3 tails, the two chromodomains of CHD1 cooperate to interact with one methylated H3 tail. We show that the human CHD1 double chromodomains target the lysine 4-methylated histone H3 tail (H3K4me), a hallmark of active chromatin9. Methylammonium recognition involves two aromatic residues, not the three-residue aromatic cage used by chromodomains of HP1 and Polycomb proteins10,11,12,13. Furthermore, unique inserts within chromodomain 1 of CHD1 block the expected site of H3 tail binding seen in HP1 and Polycomb, instead directing H3 binding to a groove at the inter-chromodomain junction.Keywords
This publication has 26 references indexed in Scilit:
- Distinct activities of CHD1 and ACF in ATP-dependent chromatin assemblyNature Structural & Molecular Biology, 2005
- The many colours of chromodomainsBioEssays, 2004
- Histone H3 lysine 4 methylation patterns in higher eukaryotic genesNature, 2003
- Identification and Analysis of Chromodomain-Containing Proteins Encoded in the Mouse TranscriptomeGenome Research, 2003
- The dMi-2 chromodomains are DNA binding modules important for ATP-dependent nucleosome mobilizationThe EMBO Journal, 2002
- Structure of HP1 Chromodomain Bound to a Lysine 9-Methylated Histone H3 TailScience, 2002
- Chromatin deacetylation by an ATP-dependent nucleosome remodelling complexNature, 1998
- The Dermatomyositis-Specific Autoantigen Mi2 Is a Component of a Complex Containing Histone Deacetylase and Nucleosome Remodeling ActivitiesCell, 1998
- Characterization of the CHD family of proteinsProceedings of the National Academy of Sciences of the United States of America, 1997
- CHD1 is concentrated in interbands and puffed regions of Drosophila polytene chromosomes.Proceedings of the National Academy of Sciences of the United States of America, 1996