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Related Concept Videos

Histone Modification02:32

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,...
Histone Modification02:32

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,...
Spreading of Chromatin Modifications02:25

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...
Heterochromatin02:38

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...
Chromatin Modification in iPS Cells01:32

Chromatin Modification in iPS Cells

Chromatin modification alters gene expression; therefore, scientists can add histone-modifying enzymes, histone variants, and chromatin remodeling complexes to somatic cells to aid reprogramming into pluripotent stem (iPS) cells.
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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...

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Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis
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Extensive histone post-translational modification in honey bees.

Mark J Dickman1, Robert Kucharski, Ryszard Maleszka

  • 1Department of Chemical and Biological Engineering, ChELSI Institute, University of Sheffield, Mappin Street, Sheffield S1 3JD, United Kingdom. m.dickman@sheffield.ac.uk

Insect Biochemistry and Molecular Biology
|November 24, 2012
PubMed
Summary

This study identifies extensive histone post-translational modifications (PTMs) in honey bees (Apis mellifera), revealing key acetylation and methylation patterns. These findings offer the first comprehensive epigenetic insights into this vital social insect.

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Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis
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Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
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Area of Science:

  • Epigenetics
  • Insect Biology
  • Molecular Biology

Background:

  • Histone post-translational modifications (PTMs) regulate eukaryotic gene expression.
  • Little is known about histone PTMs in the honey bee (Apis mellifera), an important insect pollinator.

Purpose of the Study:

  • To identify and quantify histone PTMs in the honey bee.
  • To characterize combinatorial patterns of histone PTMs in different honey bee tissues.

Main Methods:

  • Mass spectrometry was used to analyze histones H3.1, H3.3, and H4.
  • Histones were isolated from queen ovaries and 96-hour-old larvae.
  • 23 specific modification states on 23 distinct peptides were quantified.

Main Results:

  • Extensive lysine acetylation and methylation were observed on honey bee histones.
  • Detailed combinatorial information on PTMs residing on the same peptide was generated.
  • Similar PTM profiles were found in both queen ovaries and larvae, with notable differences in H3K27 and H3K36 methylation patterns.

Conclusions:

  • This study provides the first comprehensive dataset of histone PTMs in the honey bee.
  • The findings establish the honey bee as a model for studying insect epigenetics.
  • Identified PTMs offer insights into transcriptional regulation in this eusocial insect.