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Related Concept Videos

Histone Modification02:32

Histone Modification

17.0K
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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Histone Modification02:32

Histone Modification

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Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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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.
Writers
The writer...
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Synergistic Modification Induced Specific Recognition between Histone and TRIM24 via Fluctuation Correlation Network

Jinmai Zhang1, Huajie Luo2, Hao Liu1

  • 1State Key Laboratory of Microbial metabolism, Department of Bioinformatics and Biostatistics, College of Life Sciences and Biotechnology, Shanghai Jiaotong University, 800 Dongchuan Road, Shanghai, 200240, China.

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This study reveals how TRIM24 recognizes histone modifications using dynamic correlation networks. A novel "synergistic modification induced recognition" hypothesis explains TRIM24 binding mechanisms for gene regulation.

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Author Spotlight: Enhanced Histone PTM Isomer Identification Through LC-TIMS-ToF MS/MS and PASEF
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Area of Science:

  • Molecular Biology
  • Systems Biology
  • Epigenetics

Background:

  • Histone modifications are crucial for gene regulation and expression.
  • TRIM24 functions as a histone reader, recognizing specific histone modifications.
  • The precise mechanism of TRIM24 recognition of histone modifications remains unclear.

Purpose of the Study:

  • To elucidate the specific recognition mechanism between TRIM24 and histone modifications.
  • To investigate the role of histone modifications in TRIM24 binding.
  • To explore potential recognition pathways utilized by TRIM24.

Main Methods:

  • Employed a systems biology approach utilizing dynamic correlation networks.
  • Performed molecular dynamics simulations to analyze protein-histone interactions.
  • Utilized network analysis, including community analysis and shortest path search, for H3K23ac.

Main Results:

  • Dynamic correlation network analysis revealed distinct differences for H3K23ac compared to wild type and other modifications.
  • A hypothesis of "synergistic modification induced recognition" was proposed to explain TRIM24 binding.
  • Network perturbation and mutation analyses confirmed these observations, identifying significant differences in recognition pathways due to methylation and acetylation.

Conclusions:

  • Dynamic network-based analysis provides a powerful strategy for studying protein post-translational modification recognition.
  • The proposed "synergistic modification induced recognition" mechanism offers new insights into TRIM24's function.
  • Understanding these mechanisms is vital for deciphering gene regulation and expression.