skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Double chromodomains cooperate to recognize the methylated histone H3 tail

Abstract

Chromodomains are modules implicated in the recognition of lysine-methylated histone tails and nucleic acids. 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 domain. The Drosophila CHD1 localizes to the interbands and puffs of the polytene chromosomes, which are classic sites of transcriptional activity. Other CHD isoforms (CHD3/4 or Mi-2) are important for nucleosome remodelling in histone deacetylase complexes. Deletion of chromodomains impairs nucleosome binding and remodelling by CHD proteins. 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 chromatin. Methylammonium recognition involves two aromatic residues, not the three-residue aromatic cage used by chromodomains of HP1 and Polycomb proteins. 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 themore » inter-chromodomain junction.« less

Authors:
; ; ; ; ; ; ; ;  [1]
  1. ANL/SBC
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE
OSTI Identifier:
1008618
Resource Type:
Journal Article
Journal Name:
Nature
Additional Journal Information:
Journal Volume: 438; Journal Issue: 12, 2005
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; AROMATICS; CHROMATIN; CHROMOSOMES; DROSOPHILA; HISTONES; LYSINE; NUCLEIC ACIDS; NUCLEOSOMES; PROTEINS; RESIDUES; TARGETS

Citation Formats

Flanagan, John F, Mi, Li-Zhi, Chruszcz, Maksymilian, Cymborowski, Marcin, Clines, Katrina L, Kim, Youngchang, Minor, Wladek, Rastinejad, Fraydoon, Khorasanizadeh, Sepideh, and UV). Double chromodomains cooperate to recognize the methylated histone H3 tail. United States: N. p., 2010. Web.
Flanagan, John F, Mi, Li-Zhi, Chruszcz, Maksymilian, Cymborowski, Marcin, Clines, Katrina L, Kim, Youngchang, Minor, Wladek, Rastinejad, Fraydoon, Khorasanizadeh, Sepideh, & UV). Double chromodomains cooperate to recognize the methylated histone H3 tail. United States.
Flanagan, John F, Mi, Li-Zhi, Chruszcz, Maksymilian, Cymborowski, Marcin, Clines, Katrina L, Kim, Youngchang, Minor, Wladek, Rastinejad, Fraydoon, Khorasanizadeh, Sepideh, and UV). 2010. "Double chromodomains cooperate to recognize the methylated histone H3 tail". United States.
@article{osti_1008618,
title = {Double chromodomains cooperate to recognize the methylated histone H3 tail},
author = {Flanagan, John F and Mi, Li-Zhi and Chruszcz, Maksymilian and Cymborowski, Marcin and Clines, Katrina L and Kim, Youngchang and Minor, Wladek and Rastinejad, Fraydoon and Khorasanizadeh, Sepideh and UV)},
abstractNote = {Chromodomains are modules implicated in the recognition of lysine-methylated histone tails and nucleic acids. 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 domain. The Drosophila CHD1 localizes to the interbands and puffs of the polytene chromosomes, which are classic sites of transcriptional activity. Other CHD isoforms (CHD3/4 or Mi-2) are important for nucleosome remodelling in histone deacetylase complexes. Deletion of chromodomains impairs nucleosome binding and remodelling by CHD proteins. 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 chromatin. Methylammonium recognition involves two aromatic residues, not the three-residue aromatic cage used by chromodomains of HP1 and Polycomb proteins. 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.},
doi = {},
url = {https://www.osti.gov/biblio/1008618}, journal = {Nature},
number = 12, 2005,
volume = 438,
place = {United States},
year = {Mon Jul 19 00:00:00 EDT 2010},
month = {Mon Jul 19 00:00:00 EDT 2010}
}