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Related Concept Videos

Nucleosome Remodeling02:54

Nucleosome Remodeling

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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...
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Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
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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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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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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
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
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The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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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.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...
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Related Experiment Video

Updated: Dec 15, 2025

Generation and Purification of Human INO80 Chromatin Remodeling Complexes and Subcomplexes
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Generation and Purification of Human INO80 Chromatin Remodeling Complexes and Subcomplexes

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Structural Insights into the Evolutionarily Conserved BAF Chromatin Remodeling Complex.

Ryan D Marcum1, Alexis A Reyes1,2, Yuan He1,2,3

  • 1Department of Molecular Biosciences, Northwestern University, 2205 Tech Drive, Evanston, IL 60208-3500, USA.

Biology
|July 8, 2020
PubMed
Summary
This summary is machine-generated.

The switch/sucrose nonfermentable (SWI/SNF) complex regulates chromatin accessibility and is crucial for cellular processes. Mutations in SWI/SNF subunits are common in human cancers, indicating its role in tumor suppression.

Keywords:
BAF complexSWI/SNF complexcancerchromatin remodelingcryo-EM

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Last Updated: Dec 15, 2025

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Biochemical Assays for Analyzing Activities of ATP-dependent Chromatin Remodeling Enzymes
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Biochemical Assays for Analyzing Activities of ATP-dependent Chromatin Remodeling Enzymes

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Area of Science:

  • Molecular Biology
  • Genetics
  • Cancer Biology

Background:

  • The switch/sucrose nonfermentable (SWI/SNF) protein family regulates chromatin accessibility, impacting essential cellular processes.
  • Mutations in SWI/SNF subunits are frequently identified in human cancers, suggesting a tumor suppressor role.
  • Recent structural studies have elucidated the assembly and nucleosomal interactions of yeast SWI/SNF and human BAF (BRG1/BRM associated factor) complexes.

Purpose of the Study:

  • To review structural conservation between yeast SWI/SNF and human BAF complexes.
  • To examine the functional impact of cancer-associated mutations on SWI/SNF/BAF subunit function.

Main Methods:

  • Comparative structural analysis of yeast SWI/SNF and human BAF.
  • Review of exome sequencing data identifying SWI/SNF mutations in cancer.
  • Analysis of existing literature on SWI/SNF/BAF complex assembly and function.

Main Results:

  • High structural conservation exists between yeast SWI/SNF and human BAF complexes.
  • Specific SWI/SNF/BAF subunits are frequently mutated in human cancers.
  • Cancer-associated mutations may impair the chromatin remodeling function of the BAF complex.

Conclusions:

  • SWI/SNF/BAF complexes are critical for cellular function and cancer suppression.
  • Understanding the structural basis of BAF complex function is essential for interpreting cancer-associated mutations.
  • Further research into the role of mutated SWI/SNF/BAF subunits may reveal new therapeutic strategies for cancer.