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Related Concept Videos

Histone Modification02:32

Histone Modification

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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
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
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Phase II Reactions: Methylation Reactions01:17

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Methylation is a phase II biotransformation process involving the attachment of a methyl group to a substrate. Enzymes known as methyltransferases orchestrate this reaction.
The mechanism of methylation unfolds in two stages. The first stage sees a methyltransferase enzyme facilitating the transfer of a methyl group from S-adenosylmethionine (SAM) to the substrate, forming S-adenosylhomocysteine (SAH). The second stage involves further metabolism of SAH into homocysteine, which can be recycled...
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Histone Variants at the Centromere02:30

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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...
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Position-effect Variegation02:32

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In 1928, a German botanist Emil Heitz observed the moss nuclei with a DNA binding dye. He observed that while some chromatin regions decondense and spread out in the interphase nucleus, others do not. He termed them euchromatin and heterochromatin, respectively. He proposed that the heterochromatin regions reflect a functionally inactive state of the genome. It was later confirmed that heterochromatin is transcriptionally repressed, and euchromatin is transcriptionally active chromatin.
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Heterochromatin02:38

Heterochromatin

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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...
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Sulfur Assimilation01:20

Sulfur Assimilation

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Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to...
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Related Experiment Video

Updated: Jul 17, 2025

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
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Putting a finger on histidine methylation.

Paul L Boutz1

  • 1Department of Biochemistry and Biophysics, Center for RNA Biology, Center for Biomedical Informatics, Wilmot Cancer Institute, University of Rochester School of Medicine and Dentistry, Rochester, New York 14620, USA paul_boutz@urmc.rochester.edu.

Genes & Development
|September 6, 2023
PubMed
Summary

CARNMT1 is a novel enzyme that methylates histidine in both small molecules like carnosine and proteins. This dual methylation impacts RNA processing and is crucial for mammalian development.

Keywords:
CARNMT1U2AF1degradationembryonic developmentembryonic lethalityhistidinemRNAmethylationmethyltransferasesplicingzinc finger protein

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A Mass Spectrometry-Based Proteomics Approach for Global and High-Confidence Protein R-Methylation Analysis
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Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
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Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Developmental Biology

Background:

  • Enzymes methylate histidine residues on amino acids, altering protein function.
  • Histidine methylation impacts the chemical properties of the imidazole ring.

Purpose of the Study:

  • To discover novel enzymes involved in histidine methylation.
  • To understand the function of CARNMT1 in modifying peptides and proteins.

Main Methods:

  • Enzyme assays to identify histidine methyltransferase activity.
  • Mass spectrometry to identify protein and peptide targets of CARNMT1.
  • Analysis of RNA processing and metabolism in mammalian development.

Main Results:

  • CARNMT1 identified as a dual-specificity histidine methyltransferase.
  • CARNMT1 modifies the dipeptide carnosine and proteins with C3H zinc finger motifs.
  • CARNMT1 regulates RNA processing and metabolism.

Conclusions:

  • CARNMT1 plays a critical role in mammalian development.
  • Histidine methylation by CARNMT1 affects protein activity and RNA metabolism.