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Related Concept Videos

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
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Epigenetic Regulation01:37

Epigenetic Regulation

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Epigenetic changes alter the physical structure of the DNA without changing the genetic sequence and often regulate whether genes are turned on or off. This regulation ensures that each cell produces only proteins necessary for its function. For example, proteins that promote bone growth are not produced in muscle cells. Epigenetic mechanisms play an essential role in healthy development. Conversely, precisely regulated epigenetic mechanisms are disrupted in diseases like cancer.
X-chromosome...
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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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Inheritance of Chromatin Structures03:17

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Epigenetics is the study of inherited changes in a cell's phenotype without changing the DNA sequences. It provides a form of memory for the differential gene expression pattern to maintain cell lineage, position-effect variegation, dosage compensation, and maintenance of chromatin structures such as telomeres and centromeres. For example, the structure and location of the centromere on chromosomes are epigenetically inherited. Its functionality is not dictated or ensured by the underlying...
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RNA Polymerase II Accessory Proteins02:36

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Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
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Related Experiment Video

Updated: Aug 22, 2025

Immunostaining for DNA Modifications: Computational Analysis of Confocal Images
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Immunostaining for DNA Modifications: Computational Analysis of Confocal Images

Published on: September 7, 2017

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Proteins That Read DNA Methylation.

Ke Liu1, Takashi Shimbo2, Xiaosheng Song1

  • 1Hubei Key Laboratory of Genetic Regulation and Integrative Biology, School of Life Sciences, Central China Normal University, Wuhan, PR China.

Advances in Experimental Medicine and Biology
|November 9, 2022
PubMed
Summary
This summary is machine-generated.

DNA methylation alters protein binding, influencing gene expression and chromatin structure. Methyl-DNA-binding proteins utilize unique domains (MBD, SRA, TF families) for recognition, transmitting biological information.

Keywords:
DNA methylationEpigeneticsMBDMethylcytosine-binding proteins (MBPs)

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Methyl-binding DNA capture Sequencing for Patient Tissues
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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Structural Biology

Background:

  • Cytosine methylation is a key epigenetic modification affecting DNA-protein interactions.
  • This modification alters DNA's major groove, impacting the binding affinity and specificity of DNA-binding proteins.
  • Methylated DNA recognition by proteins initiates regulatory events influencing gene expression and chromatin structure.

Purpose of the Study:

  • To summarize structural and biochemical analyses of DNA methylation recognition mechanisms.
  • To correlate these mechanisms with emerging genomic and functional data on methyl-DNA-binding proteins.
  • To elucidate the unique features and functions of methyl-DNA-binding proteins.

Main Methods:

  • Structural analyses of methyl-DNA-binding protein domains.
  • Biochemical studies on DNA methylation recognition.
  • Review of recent genetic and genomic studies on methyl-DNA-binding proteins.

Main Results:

  • Methyl-DNA-binding proteins recognize DNA methylation through distinct domains: MBD, SRA, and various TF families (e.g., C2H2 zinc finger, bHLH, bZIP, homeodomain).
  • Each domain exhibits unique methylated DNA-binding patterns and recognition mechanisms, enabling the transmission of complex biological information.
  • Emerging genomic and functional data reveal novel roles and unique features of these proteins.

Conclusions:

  • Methyl-DNA-binding proteins play crucial roles in regulating gene expression and chromatin structure through specific recognition of DNA methylation.
  • The diverse recognition mechanisms employed by different protein domains highlight the sophisticated biological information encoded by DNA methylation.
  • Continued research into these proteins promises further insights into epigenetic regulation and cellular function.