Methods to identify and functionally analyze factors that specifically recognize histone lysine methylation.
Robert J Sims1, Patrick Trojer, Guohong Li
1Division of Nucleic Acids Enzymology, Department of Biochemistry, Robert Wood Johnson Medical School Piscataway, NJ 08854-5635, USA.
Methods (San Diego, Calif.)
|November 15, 2006
Summary
Histone lysine methylation regulates gene expression and cellular identity. This study explores methods to investigate histone methyl-recognition and its functional impact on transcription.
Area of Science:
- Molecular Biology
- Epigenetics
- Gene Regulation
Background:
- Histone lysine methylation is crucial for gene expression and cellular identity.
- The downstream effects of histone methyl-recognition are not fully understood.
- Investigating these mechanisms is vital for understanding fundamental biological processes.
Purpose of the Study:
- To describe methods for investigating specific histone lysine-methyl recognition.
- To discuss techniques for assessing the functional consequences of this recognition.
- To provide a comprehensive overview of current research approaches.
Main Methods:
- Utilizing short peptides to study histone methyl-recognition.
- Employing histone octamers for in-depth analysis.
- Using nucleosomal arrays for a more physiological context.
- Applying techniques to assess binding and transcriptional regulation.
Main Results:
- The study outlines diverse methodologies for probing histone methyl-recognition.
- It highlights the importance of using different model systems (peptides, octamers, nucleosomal arrays).
- Techniques for evaluating functional outcomes related to transcription are presented.
Conclusions:
- Effective methods exist to investigate histone lysine-methyl recognition.
- Understanding these mechanisms is key to deciphering gene regulation.
- Further research using these techniques will advance epigenetic studies.
Related Concept Videos
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,...
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...


