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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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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.
These groups modify specific amino acids in a protein....
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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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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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Cooperative Binding of Transcription Regulators02:13

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Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form...
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Gene transcription is regulated by the synergistic action of several proteins that form a complex at a gene regulatory site. This is observed in eukaryotes, where the regulation of gene expression is a complex process. Regulatory proteins in eukaryotes can broadly be classified into two types – regulators that bind directly to specific DNA sequences and co-regulators that associate with regulatory proteins but cannot directly bind to the DNA. These co-regulators are further divided into...
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Related Experiment Video

Updated: May 1, 2026

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
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In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

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Two-way communications between ubiquitin-like modifiers and DNA.

Helle D Ulrich1

  • 11] Institute of Molecular Biology, Mainz, Germany. [2].

Nature Structural & Molecular Biology
|April 5, 2014
PubMed
Summary

This review explores how DNA influences ubiquitin and SUMO modifications, and how these modifications, in turn, affect DNA binding. Understanding these interactions is key to regulating nucleic acid metabolism.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Post-translational modifications by ubiquitin and SUMO regulate critical nucleic acid metabolic processes like DNA replication, repair, and transcription.
  • DNA structure and sequence are integral in directing the modification of chromatin-associated proteins.
  • Protein ubiquitination or SUMOylation can significantly alter their DNA-binding capabilities.

Purpose of the Study:

  • To elucidate the mechanistic principles governing the interplay between DNA and the post-translational modifiers ubiquitin and SUMO.
  • To provide a comprehensive overview of how DNA and these modification systems mutually influence each other.

Main Methods:

  • This review synthesizes existing literature and mechanistic studies.
  • It focuses on the reciprocal regulatory mechanisms between DNA and ubiquitin/SUMO pathways.

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Author Spotlight: Quantitative Detection of DNA Protein Crosslinks and Their Post-Translational Modifications
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Related Experiment Videos

Last Updated: May 1, 2026

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Main Results:

  • DNA influences the ubiquitination and SUMOylation status of chromatin-associated proteins.
  • Ubiquitination and SUMOylation impact the DNA-binding affinity and specificity of proteins.
  • These interactions form a regulatory network crucial for nucleic acid metabolism.

Conclusions:

  • The dynamic interplay between DNA and ubiquitin/SUMO systems is fundamental for regulating gene expression and genome stability.
  • Further research into these mechanisms can reveal novel therapeutic targets for diseases involving aberrant nucleic acid metabolism.