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PMID: 17984965 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Review

How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers.

Nature structural & molecular biology ·Vol. 14 ·No. 11 ·2007-11-00 ·Pages 1025-1040

Taverna SD, Li H, Ruthenburg AJ, Allis CD, Patel DJ

Abstract

Histones comprise the major protein component of chromatin, the scaffold in which the eukaryotic genome is packaged, and are subject to many types of post-translational modifications (PTMs), especially on their flexible tails. These modifications may constitute a 'histone code' and could be used to manage epigenetic information that helps extend the genetic message beyond DNA sequences. This proposed code, read in part by histone PTM-binding 'effector' modules and their associated complexes, is predicted to define unique functional states of chromatin and/or regulate various chromatin-templated processes. A wealth of structural and functional data show how chromatin effector modules target their cognate covalent histone modifications. Here we summarize key features in molecular recognition of histone PTMs by a diverse family of 'reader pockets', highlighting specific readout mechanisms for individual marks, common themes and insights into the downstream functional consequences of the interactions. Changes in these interactions may have far-reaching implications for human biology and disease, notably cancer.

MeSH Terms
14-3-3 Proteins/chemistry,metabolism Adaptor Proteins, Signal Transducing Amino Acids/chemistry,metabolism Cell Cycle Proteins Chromatin/chemistry,metabolism DNA-Binding Proteins/chemistry,metabolism Epigenesis, Genetic Histone Acetyltransferases Histones/chemistry,metabolism Humans Models, Molecular Nuclear Proteins/chemistry,metabolism Protein Conformation Protein Processing, Post-Translational Protein Structure, Tertiary TATA-Binding Protein Associated Factors/chemistry,metabolism Trans-Activators/chemistry,metabolism Transcription Factor TFIID/chemistry,metabolism p300-CBP Transcription Factors/chemistry,metabolism
Chemicals
14-3-3 Proteins Adaptor Proteins, Signal Transducing Amino Acids Cell Cycle Proteins Chromatin DNA-Binding Proteins H2AX protein, human Histones MDC1 protein, human Nuclear Proteins TATA-Binding Protein Associated Factors Trans-Activators Transcription Factor TFIID Histone Acetyltransferases p300-CBP Transcription Factors p300-CBP-associated factor TATA-binding protein associated factor 250 kDa
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Taverna Sean D
Laboratory of Chromatin Biology, The Rockefeller University, New York, New York 10021, USA.
Li Haitao
Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
Ruthenburg Alexander J
Laboratory of Chromatin Biology, The Rockefeller University, New York, New York 10021, USA.
Allis C David
Laboratory of Chromatin Biology, The Rockefeller University, New York, New York 10021, USA.
Patel Dinshaw J
Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
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Article Info
Journal
Nature structural & molecular biology
Abbr.
Nat Struct Mol Biol
ISSN
1545-9985
Published
2007-11-00
Epub
2007-00-05
Pages
1025-1040
Language
English
Region
United States
NLM ID
101186374
PMCID
PMC4691843
Subset
IM
Grants
NCI NIH HHS · P30 CA008748 · United States
NIGMS NIH HHS · R01 GM063959 · United States
NIGMS NIH HHS · GM63959 · United States
NIGMS NIH HHS · R37 GM053512 · United States
NIGMS NIH HHS · GM53512 · United States
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