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.

RefeRences

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