Related Experiment Video
Updated: Aug 16, 2026

08:44
Generation and Purification of Human INO80 Chromatin Remodeling Complexes and Subcomplexes
Published on: October 23, 2014
Anything else but GAGA: a nonhistone protein complex reshapes chromatin structure
1University of Arkansas, Department of Biological Sciences, Fayetteville, AR 72701, USA. mlehmann@uark.edu
Trends in Genetics : TIG
|December 31, 2003
Summary
DNA packaging in the nucleus is controlled by chromatin structure. GAGA-binding proteins in fruit flies remodel nucleosomes, influencing gene regulation and homeotic gene expression.
Area of Science:
- Molecular Biology
- Genetics
- Epigenetics
Background:
- DNA packaging within the cell nucleus presents challenges and control mechanisms for essential genetic processes.
- Dynamic alterations in chromatin's nucleosome structure are critical for gene expression regulation, including activation and silencing.
- Changes in higher-order chromatin architecture are hypothesized to be linked to nucleosome modifications, though poorly understood.
Purpose of the Study:
- To summarize recent findings on the composition and architecture of GAGA-binding protein complexes.
- To discuss the role of these complexes in regulating homeotic gene expression.
Main Methods:
- Studies in Drosophila melanogaster.
- Analysis of protein complexes binding to GAGA DNA elements.
- Investigating nucleosome replacement and chromatin environment modification.
Main Results:
- GAGA-binding protein complexes can replace nucleosomes.
- This replacement creates a local chromatin environment facilitating regulatory responses.
- These complexes play a multifaceted role in homeotic gene regulation.
Conclusions:
- GAGA-binding proteins are key players in modulating chromatin structure for gene regulation.
- Understanding GAGA-binding complexes offers insights into the control of homeotic gene expression.
Related Concept Videos
Nucleosome Remodeling
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.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
Histone Modification
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Spreading 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.
Writers
The writer is an enzyme that can...
Writers
The writer is an enzyme that can...
Heterochromatin
The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at 9th...
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at 9th...
Heterochromatin
The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at 9th...
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at 9th...
Histone Modification
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...

