Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Cooperative Binding of Transcription Regulators

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome. Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form...

Cooperative Binding of Transcription Regulators

Cooperative Binding of Transcription Regulators

Chromatin Structure Regulates pre-mRNA Processing

Chromatin Structure Regulates pre-mRNA Processing

In eukaryotic cells, nascent mRNA transcripts need to undergo many post-transcriptional modifications to reach the cell cytoplasm and translate into functional proteins. For a long time, transcription and pre-mRNA processing were considered two independent events that occur sequentially in the cell. However, it has now been well established that transcription and pre-mRNA processing are two simultaneous processes that are precisely regulated inside the cell.
The chromatin structure, especially...

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....

Ligand Binding and Linkage

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...

Assembly of Complex Microtubule Structures

Assembly of Complex Microtubule Structures

Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Physical interactions within the SIR heterochromatin complex potentiate inter-subunit communication and gene repression.

Cell reports·2026

Same author

EZH2 Serine 21 Phosphorylation Restrains Compact-State PRC2 Activation and H3K27me3 Propagation.

bioRxiv : the preprint server for biology·2026

Same author

Structure of the human HIRA histone chaperone with a nucleosome suggests a stepwise nucleosome assembly mechanism.

bioRxiv : the preprint server for biology·2026

Same author

RNA-induced PRC2 inhibition depends on the sequence of bound RNA.

Nature communications·2026

Same author

RNA-induced PRC2 inhibition depends on the sequence of bound RNA.

Research square·2025

Same author

The mitochondrial disulphide relay substrate FAM136A safeguards IMS proteostasis and cellular fitness.

Redox biology·2025

Search research articles

Related Experiment Video

Updated: Feb 2, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

Recent Structural Insights into Polycomb Repressive Complex 2 Regulation and Substrate Binding.

Vignesh Kasinath^1,2, Simon Poepsel^1,2, Eva Nogales^1,2,3,4

¹California Institute for Quantitative Biosciences (QB3) , University of California , Berkeley , California 94720 , United States.

|November 20, 2018

Summary

This summary is machine-generated.

Polycomb repressive complex 2 (PRC2) is crucial for gene regulation. Recent structural studies reveal how its assembly and activity, particularly histone H3 lysine 27 trimethylation (H3K27me3), establish repressive chromatin domains.

More Related Videos

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

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

Published on: October 2, 2017

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

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

Published on: March 10, 2021

Related Experiment Videos

Last Updated: Feb 2, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

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

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

Published on: October 2, 2017

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

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

Published on: March 10, 2021

Area of Science:

Epigenetics and Gene Regulation
Molecular Biology
Structural Biology

Background:

Polycomb group proteins are key transcriptional repressors.
Chromatin-modifying enzymes, like Polycomb repressive complex 2 (PRC2), regulate gene expression through histone and DNA modifications.
PRC2 catalyzes histone H3 lysine 27 trimethylation (H3K27me3), a mark associated with gene silencing and cell identity maintenance.

Purpose of the Study:

To review recent structural biology studies on PRC2.
To elucidate the molecular mechanisms governing PRC2 activity and regulation.
To understand how H3K27me3 spreading establishes repressive chromatin domains.

Main Methods:

Structural biology techniques (e.g., X-ray crystallography, cryo-EM).
Biochemical assays to study enzyme activity.
Analysis of intersubunit interactions within PRC2.

Main Results:

Structural insights into PRC2 complex assembly and stability.
Understanding the regulation of PRC2 methyltransferase activity through structural mechanisms.
Elucidation of the mechanism of H3K27me3 spreading and domain formation.

Conclusions:

Structural studies are vital for understanding PRC2 function in gene silencing.
Intersubunit interactions play critical roles in PRC2 assembly and activity regulation.
PRC2-mediated H3K27me3 spreading is a key mechanism for establishing transcriptionally repressive domains.