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Related Concept Videos

Nucleosome Remodeling02:54

Nucleosome Remodeling

Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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 is an enzyme that can...
Epigenetic Regulation01:37

Epigenetic Regulation

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...
Epigenetic Regulation01:46

Epigenetic Regulation

Epigenetic mechanisms play an essential role in healthy development. Conversely, precisely regulated epigenetic mechanisms are disrupted in diseases like cancer.
Histone Modification02:32

Histone Modification

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 deacetylase,...
Histone Modification02:32

Histone Modification

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 deacetylase,...

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Updated: May 24, 2026

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
06:32

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Published on: March 9, 2022

A revised model for PHF20L1 Tudor function: DNA binding overrides methylation selectivity on nucleosomes.

Xiaolei Huang1, Qin Xiao1, Xin Liu2

  • 1Jiangsu Key Laboratory of Drug Discovery and Translational Research for Brain Diseases, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu, China; Jiangsu Province Engineering Research Center of Precision Diagnostics and Therapeutics Development, Soochow University, Suzhou, Jiangsu, China; College of Pharmaceutical Sciences, Suzhou International Joint Laboratory for Diagnosis and Treatment of Brain Diseases, Soochow University, Suzhou, Jiangsu, China.

The Journal of Biological Chemistry
|May 22, 2026
PubMed
Summary
This summary is machine-generated.

Plant homeodomain finger protein 20-like protein 1 (PHF20L1) Tudor domains selectively bind methylated histones. However, PHF20L1

Keywords:
Tudor domainhistone bindingmethyl-lysinenucleosome binding PHF20L1

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Area of Science:

  • * Molecular Biology
  • * Epigenetics
  • * Structural Biology

Background:

  • * Plant homeodomain finger protein 20-like protein 1 (PHF20L1) functions as a methyl-lysine reader, influencing chromatin remodeling and transcription.
  • * Its tandem Tudor and PHD finger domains are key to its regulatory role.

Purpose of the Study:

  • * To characterize the selectivity of PHF20L1's Tudor domains for methylated lysine residues.
  • * To elucidate the structural basis of this selectivity.
  • * To investigate the binding mechanism of PHF20L1 to chromatin.

Main Methods:

  • * Biophysical techniques: Quantitative fluorescence polarization (FP) and isothermal titration calorimetry (ITC).
  • * Structural biology: X-ray crystallography.
  • * Functional assays: Nucleosome binding assays.

Main Results:

  • * Tudor1 exhibits modest preference for H3K36me1 over H4K20me1/2; Tudor2 is specific for H4K20me2.
  • * Tandem Tudor domains show cooperative binding to H3K36me.
  • * Crystal structures reveal specific interactions within aromatic cages that dictate selectivity.
  • * PHF20L1's tandem Tudor domains bind DNA with high affinity, losing methylation selectivity on nucleosomes.

Conclusions:

  • * PHF20L1's Tudor domains possess distinct methylation specificities, fine-tuned by aromatic cage architecture and acidic residue interactions.
  • * The tandem arrangement enhances affinity for specific methylated histone marks.
  • * Contrary to expectations, PHF20L1 functions as a high-affinity DNA-binding module on nucleosomes, rather than solely a selective methyl-lysine reader.
  • * This study redefines the mechanistic framework of PHF20L1's chromatin engagement.