Related Experiment Video
Updated: Dec 29, 2025

07:26
Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
Published on: December 26, 2020
4.3K
Revealing eukaryotic histone-modifying mechanisms through bacterial infection
Wenyang Dong1,2, Melanie Anne Hamon3
1G5 Chromatine et Infection, Institut Pasteur, 75015, Paris, France.
Seminars in Immunopathology
|February 6, 2020
Summary
Bacteria manipulate host transcription by altering histone modifications. This review explores bacterial strategies for inducing histone post-translational modifications (PTMs) and their impact on host cell biology.
Area of Science:
- Microbiology
- Molecular Biology
- Epigenetics
Background:
- Host-pathogen interactions involve bacterial manipulation of host cell transcription.
- Histone post-translational modifications (PTMs) are key regulators of gene expression and are targeted during infection.
Purpose of the Study:
- To review bacterial mechanisms for inducing histone PTMs.
- To summarize cell biology insights gained from studying bacteria-induced histone modifications.
Main Methods:
- Focus on bacteria-induced histone modifications.
- Discussion of direct targeting of pathogen effector enzymes.
- Analysis of indirect modulation of cellular signaling cascades.
Main Results:
- Bacteria employ diverse strategies to induce histone PTMs.
- Bacterial effectors directly target histones or modulate signaling pathways.
- Novel histone marks are imposed upon infection, revealing host cell regulatory mechanisms.
Conclusions:
- Studying bacteria-induced histone modifications enhances understanding of virulence and host cell biology.
- Bacterial manipulation of chromatin offers insights into signaling cascades and enzyme mimicry.
More Related Videos
Related Concept Videos
Histone Modification
15.7K
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...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
15.7K
Histone Modification
4.2K
4.2K
Spreading of Chromatin Modifications
9.2K
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...
Writers
The writer...
9.2K
Nucleosome Remodeling
10.6K
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...
10.6K
The Nucleosome Core Particle
2.0K
Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
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...
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...
2.0K
The Nucleosome Core Particle
13.9K
Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
13.9K

