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Generation and Purification of Human INO80 Chromatin Remodeling Complexes and Subcomplexes
Published on: October 23, 2014
Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex
J K Tong1, C A Hassig, G R Schnitzler
1Howard Hughes Medical Institute, Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
Nature
|November 6, 1998
Summary
Researchers discovered a new nucleosome remodelling and deacetylating (NRD) complex in human cells. This complex links histone deacetylase and ATP-dependent nucleosome remodelling activities, impacting gene transcription and chromatin structure.
Area of Science:
- Molecular Biology
- Epigenetics
- Chromatin Biology
Background:
- Eukaryotic chromosome dynamics, including DNA replication and gene transcription, rely on nucleosome core assembly and remodeling.
- Histone acetylation and ATP-dependent nucleosome remodeling are key enzymatic processes regulating transcription.
- Histone deacetylases (HDACs) exhibit limitations in deacetylating oligonucleosomal histones in vitro.
Purpose of the Study:
- To identify and characterize novel ATP-dependent nucleosome remodeling activities within human histone deacetylase complexes.
- To investigate the potential coupling of distinct chromatin-modifying activities.
Main Methods:
- Biochemical assays to identify and characterize ATP-dependent nucleosome remodeling activity.
- Functional analysis of histone deacetylase complexes.
- In vitro deacetylation assays using oligonucleosomal histones.
Main Results:
- Identification of a novel ATP-dependent nucleosome remodeling activity within an endogenous human histone deacetylase complex.
- This activity is attributed to CHD3 and CHD4 proteins, possessing helicase/ATPase domains.
- The identified complex, termed the nucleosome remodeling and deacetylating (NRD) complex, facilitates in vitro deacetylation of oligonucleosomal histones.
Conclusions:
- Establishes a physical and functional link between histone deacetylase and nucleosome remodeling activities.
- The NRD complex integrates distinct chromatin-modifying functions.
- Provides new insights into the regulation of transcription and chromatin structure.
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Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
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Acetylation
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02:25Spreading of Chromatin Modifications
The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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01:32Chromatin Modification in iPS Cells
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Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...
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