Related Experiment Video

Updated: Jul 15, 2026

Sequential Salt Extractions for the Analysis of Bulk Chromatin Binding Properties of Chromatin Modifying Complexes
07:41

Sequential Salt Extractions for the Analysis of Bulk Chromatin Binding Properties of Chromatin Modifying Complexes

Published on: October 2, 2017

Solution structure of BRD7 bromodomain and its interaction with acetylated peptides from histone H3 and H4

Hongbin Sun1, Jiangxin Liu, Jiahai Zhang

  • 1Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, PR China.

Biochemical and Biophysical Research Communications
|May 15, 2007
PubMed

Insights

Bromodomain-containing protein 7 (BRD7) impacts Nasopharyngeal carcinoma (NPC) progression. This study determined the BRD7 bromodomain structure and found it binds acetylated histones with low specificity, offering insights into its role in chromatin regulation.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • Bromodomain-containing protein 7 (BRD7) is implicated in Nasopharyngeal carcinoma (NPC) progression.
  • BRD7 overexpression inhibits NPC cell growth and cell cycle by regulating related genes.
  • BRD7 possesses a bromodomain crucial for chromatin remodeling and transcriptional activation.

Purpose of the Study:

  • To elucidate the solution structure of the BRD7 bromodomain.
  • To investigate the binding specificity of the BRD7 bromodomain to acetylated histone peptides.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy for structure determination.
  • NMR titration experiments with various acetylated histone peptides to assess binding.

Main Results:

  • The BRD7 bromodomain adopts a canonical left-handed four-helix bundle topology.
  • Weak affinity binding was observed with acetylated histone H3 (K9, K14) and H4 (K8, K12, K16) peptides.
  • The BRD7 bromodomain exhibits a lack of inherent binding specificity to histones in vitro.

Conclusions:

  • The structural and binding data provide a foundation for understanding BRD7's function in chromatin regulation.
  • The observed low binding specificity suggests potential roles for other domains or interactions in BRD7's biological functions.
  • Further research is needed to clarify the precise mechanisms of BRD7 in NPC pathogenesis.

More Related Videos

The Development and Application of Biophysical Assays for Evaluating Ternary Complex Formation Induced by Proteolysis Targeting Chimeras (PROTACS)07:22

The Development and Application of Biophysical Assays for Evaluating Ternary Complex Formation Induced by Proteolysis Targeting Chimeras (PROTACS)

Published on: January 12, 2024

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin11:17

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Published on: March 10, 2021

Related Concept Videos

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,...
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...
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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...
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

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.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
Electrophilic 1,2- and 1,4-Addition of HX to 1,3-Butadiene01:17

Electrophilic 1,2- and 1,4-Addition of HX to 1,3-Butadiene

The electrophilic addition of hydrogen halides such as HBr to alkenes and nonconjugated dienes gives a single product as per Markovnikov’s rule.
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...