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Related Concept Videos

Histone Variants at the Centromere02:30

Histone Variants at the Centromere

Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3 variants are also...
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...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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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In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
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In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

Published on: December 29, 2021

Structure of Vps75 and implications for histone chaperone function.

Yong Tang1, Katrina Meeth, Eva Jiang

  • 1Program in Gene Expression and Regulation, Wistar Institute, 3601 Spruce Street, Philadelphia, PA 19104, USA.

Proceedings of the National Academy of Sciences of the United States of America
|August 30, 2008
PubMed
Summary
This summary is machine-generated.

The vacuolar protein sorting 75 (Vps75) histone chaperone has a unique headphone structure. This structure facilitates histone H3-H4 binding and interaction with Rtt109 for histone acetylation.

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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
08:58

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

Area of Science:

  • Chromatin biology
  • Molecular structural biology
  • Epigenetics

Background:

  • Vacuolar protein sorting 75 (Vps75) is a histone chaperone involved in chromatin dynamics.
  • Vps75, with antisilencing factor 1, promotes histone H3-Lys-56 acetylation via Rtt109.
  • Understanding Vps75's structure-function relationship is crucial for chromatin regulation.

Purpose of the Study:

  • To determine the x-ray crystal structure of Vps75.
  • To biochemically characterize the interaction between Vps75 and Rtt109.
  • To elucidate the structural basis for Vps75's role in nucleosome assembly and histone acetylation.

Main Methods:

  • X-ray crystallography to determine Vps75 structure.
  • Biochemical assays to study Vps75-Rtt109 interactions.
  • Structural comparison with other histone chaperones.

Main Results:

  • Vps75 forms a homodimeric "headphone" architecture with unique features.
  • Two surfaces on Vps75's earmuff domain interact with Rtt109 in a 2:1 stoichiometry.
  • A central cleft in the Vps75 dimer remains accessible for histone binding.

Conclusions:

  • The Vps75 structure provides a framework for its dual role in nucleosome assembly and Rtt109-mediated histone acetylation.
  • Unique structural features of Vps75 explain its specific interactions with Rtt109.
  • Vps75's structure facilitates simultaneous histone binding and interaction with the Rtt109 acetyltransferase.