Related Experiment Video
Updated: Jul 2, 2026
11:08
A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
Lysine acetylation: codified crosstalk with other posttranslational modifications.
Xiang-Jiao Yang1, Edward Seto2
1Molecular Oncology Group, Department of Medicine, McGill University Health Centre, Montréal, QC H3A 1A1, Canada; McGill Cancer Centre, Montréal, QC H3A 1A1, Canada.
Molecular Cell
|August 30, 2008
Summary
Lysine acetylation modifies many proteins beyond histones. This review explores how acetylation interacts with other modifications to control cellular signaling and epigenetic programs.
Area of Science:
- Molecular Biology
- Epigenetics
- Cellular Signaling
Background:
- Lysine acetylation is a key posttranslational modification, primarily known for its role in histone regulation.
- It significantly influences chromatin structure, transcriptional control, and epigenetic inheritance.
- Beyond histones, numerous nonhistone proteins are also acetylated, impacting various cellular functions.
Purpose of the Study:
- To review recent findings on the acetylation of nonhistone proteins.
- To highlight the crosstalk between lysine acetylation and other posttranslational modifications.
- To emphasize the formation of multisite modification codes for dynamic cellular signaling.
Main Methods:
- Literature review of recent scientific findings.
- Analysis of studies investigating posttranslational modification crosstalk.
- Synthesis of information on acetylation's role in nonhistone proteins.
Main Results:
- Acetylation targets a wide range of nuclear and cytoplasmic proteins.
- Significant crossregulation exists between lysine acetylation and other modifications like phosphorylation, methylation, ubiquitination, and sumoylation.
- These interactions form complex "code-like" patterns regulating cellular signaling.
Conclusions:
- Lysine acetylation of nonhistone proteins is a critical regulatory mechanism.
- The interplay between different posttranslational modifications creates sophisticated signaling pathways.
- Understanding these codes is essential for comprehending dynamic cellular responses.
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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
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Acetylation
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02:32Histone Modification
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These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.
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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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X-chromosome...
X-chromosome...