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Updated: Jul 10, 2026
07:08
Detection of Histone Modifications in Plant Leaves
Published on: September 23, 2011
Distinctive core histone post-translational modification patterns in Arabidopsis thaliana
Kangling Zhang1, Vaniyambadi V Sridhar, Jianhua Zhu
1Mass Spectrometry Facility, School of Medicine, Loma Linda University, Loma Linda, California, United States of America.
Plos One
|November 22, 2007
Summary
Plant histone modifications are distinct from mammals and yeast. This study identified unique histone acetylation, phosphorylation, and ubiquitination sites in Arabidopsis thaliana, revealing plant-specific epigenetic regulation patterns.
Area of Science:
- Epigenetics and molecular biology
- Plant science research
- Chromatin regulation
Background:
- Post-translational histone modifications are vital for gene expression and epigenetic regulation.
- While conserved in mammals and yeast, plant histone modification sites remain poorly understood.
- Plants are key models for studying epigenetic regulation.
Purpose of the Study:
- To identify specific histone modification sites and patterns in the model plant Arabidopsis thaliana.
- To compare plant histone modifications with those found in mammalian and yeast systems.
- To lay the groundwork for future plant epigenetics research.
Main Methods:
- Utilized mass spectrometry coupled with high-performance liquid chromatography (HPLC) separation.
- Employed phospho-peptide enrichment techniques.
- Focused on the reference plant Arabidopsis thaliana.
Main Results:
- Identified numerous conserved and plant-unique histone modification sites.
- Discovered unique modifications including H4 K20 acetylation and various H2B, H2A, and H2A.X modifications.
- Found that H3 K79, a conserved methylation site in other systems, is unmodified in Arabidopsis.
Conclusions:
- Arabidopsis thaliana exhibits distinctive histone modification patterns compared to non-plant systems.
- These findings highlight unique plant-specific epigenetic regulatory mechanisms.
- Provides a foundational resource for investigating plant histone modifications and their roles.
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02:32Histone 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,...
02:32Histone 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,...
02:30Histone Variants at the Centromere
Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3 variants are also...
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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...
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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.
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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...
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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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The writer is an enzyme that can...
Writers
The writer is an enzyme that can...