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Bromodomain
H3/H4KacANCCA (H3K14)BDF1BRD2,3,4,7BRDT(H4K5K8; H3K18)BRG1CBP/p300 (H4K20; H3K36)GCN5 (H4K16)PB-2 (H3K14)PCAFRSC4 (H3K14)TAF1TRIM24 (H3K23)GCN5
H3K4me3/2BPTFING1,2,3,4,5JARID1AKDM7A(ce)KIAA1718LidMLL1PHF2,8PHO23PygoRAG2TAF3YNG1,2
H3unAIREBHC80CHD4DNMT3LJADE1TRIM24
H3K9meCHD4ICBP90SMCX
H3K14acDPF3
H3K4me3ZCWPW1
PHD
TandemPHD
ZF-CW
H3R2WDR5
H3/H4/H1Kme3EED
H4un (15-41)RbAp46/48
EED
WD40/β propeller
14-3-3
H3S10phH3S28ph14-3-3
14-3-3
L3MBTL1
H3/H4Kme1/2L3MBTL1,2MBTD1SCMSCML2SFMBT
H3K9me2/3LIN61
MBT
MDC1
H2AXS139phMDC1
BRCT
BRPF1 H3K36me3BRPF1DNMT3A
H4K20me1PDP1
PWWP
H4K20me253BP1CRB2
H3/H4Rme2TDRD3
H3/H4Kme3FXR1,2 (H4K20)JMJD2A (H3K4)JMJD2A (H4K20)UHRF1 (H3K9)
53BP1
Tudor/Tandem Tudor
HP1
H3K4meCHD1(h)
H3K36me3/2EAF3MRG15MSL3 (H4K20me1-DNA)
H3K9me3/2HP1CBX1,3,5CDYCHP1MPP8Tip60
H3K27me3/2Pc
H3K27/K9me3/2CBX2,4,6,7,8
DoubleChromodomain
Chromodomain Chromo Barrel
H3K9me2/1G9aGLP
GLP
Ankyrin
ING2
842 Cell 146, September 2, 2011 ©2011 Elsevier Inc. DOI 10.1016/j.cell.2011.08.022 See online version for legend and references.
SnapShot: Histone ReadersTatiana G. Kutateladze1
1Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA
SnapShot: Histone ReadersTatiana G. Kutateladze1
1Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA
842.e1 Cell 146, September 2, 2011 ©2011 Elsevier Inc. DOI 10.1016/j.cell.2011.08.022z
Posttranslational modifications (PTMs) of histone proteins and methylation of DNA are major components of the epigenetic machinery that regulates the structure and dynamics of chromatin, gene transcription, DNA replication, DNA recombination, and DNA repair. The PTMs alter direct interactions between histones and DNA and serve as docking sites for epigenetic effectors. A number of PTMs have been identified in the flexible histone tails that protrude from the nucleosomal core and are readily accessible to histone acetyltransferases (HATs), histone deacetylases (HDACs), histone lysine methyltransferases (HKMTs), kinases, phosphatases, and other enzymes capable of depositing or removing PTMs. The list of PTMs is rapidly growing and includes acetylation, methylation, ubiquitination, and SUMOylation of lysine residues, methylation and citrullination of arginine residues, phosphorylation of serine and threonine residues, and ADP-ribosylation of glutamate and arginine residues.
The histone PTMs are recognized by protein modules, referred to as epigenetic effectors, histone-binding domains, or simply “readers” of PTMs. Binding of the effectors recruits or stabilizes various transcription factors, chromatin remodeling complexes, and other components of the transcriptional network at chromatin. Many chromatin-associating proteins contain multiple copies of an effector or several different effectors, often specific for distinct PTMs. This provides a multivalent mechanism for targeting to a particular genomic site and ensures the proper biological outcome. Furthermore, the effectors are commonly found in macromolecules that either possess catalytic activities or act as scaffolding proteins that tether multisubunit enzymatic complexes to chromatin. These, in turn, further modify the epigenetic landscape by “erasing” PTMs, “writing” new epigenetic marks, or cleaving off the entire tail. This SnapShot shows the histone-binding effectors, their atomic-resolution structures, and the reported specificities for PTMs.
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