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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
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Covalently Linked Protein Regulators02:04

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Spreading of Chromatin Modifications02:25

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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 Nucleosome Core Particle01:12

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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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Non-enzymatic Covalent Modifications as a New Chapter in the Histone Code.

Igor Maksimovic1, Yael David2

  • 1Tri-Institutional PhD Program in Chemical Biology, New York, NY, USA; Chemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY, USA.

Trends in Biochemical Sciences
|May 9, 2021
PubMed
Summary

Reactive species form non-enzymatic covalent modifications (NECMs) on cellular macromolecules, impacting cell processes. This review covers NECM chemistry, chromatin effects, regulation, and chemical biology tools for studying these dynamic modifications.

Keywords:
acylationchemical biologychromatinepigeneticsglycationlipidation

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Chemical Biology

Background:

  • Cells contain reactive species that form non-enzymatic covalent modifications (NECMs) on macromolecules.
  • NECMs can disrupt cellular functions by altering protein structure, activity, and interactions.
  • Chromatin, the blueprint of the cell, is subject to dynamic NECM accumulation.

Purpose of the Study:

  • To review the chemistry of NECM formation.
  • To discuss the impact of NECMs on chromatin structure and gene transcription.
  • To explore cellular regulatory mechanisms and chemical biology tools for NECMs.

Main Methods:

  • Literature review of NECM formation and function.
  • Discussion of chromatin dynamics and transcriptional regulation.
  • Overview of chemical biology platforms for NECM analysis.

Main Results:

  • NECMs arise from reactive species and modify macromolecules, affecting cellular processes.
  • Accumulated NECMs on chromatin alter its structure and influence transcriptional output.
  • Cells possess regulatory mechanisms to prevent or reverse NECM formation.

Conclusions:

  • NECMs are significant cellular modifications impacting chromatin and transcription.
  • Understanding NECM chemistry and regulation is crucial for cell biology.
  • Chemical biology offers advanced tools to investigate and manipulate NECMs.