Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Separation of Sister Chromatids02:17

Separation of Sister Chromatids

4.3K
At the transition from prophase to metaphase, there is a reduction in cohesion along the chromosomal arms, resulting in the resolution of sister chromatids. However, residual cohesin connections remain to hold the sister chromatids together until the transition from metaphase to anaphase. The residual connection prevents any premature separation of sister chromatids, blocking the risks of aneuploidy within the daughter cells.
At the onset of anaphase, separase, a proteolytic enzyme, is...
4.3K
Caspases01:24

Caspases

13.7K
Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside...
13.7K
The Proteasome Structure01:17

The Proteasome Structure

1.6K
The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
1.6K
The Proteasome02:18

The Proteasome

10.0K
Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
10.0K
The Proteasome01:13

The Proteasome

1.6K
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
1.6K
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

3.3K
The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
3.3K

You might also read

Related Articles

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

Sort by
Same author

Investigations into multiple fission yeast chromosome size determinants.

Journal of cell science·2026
Same author

Progressive chromosome shape changes during cell divisions.

EMBO reports·2025
Same author

Author Correction: An extrinsic motor directs chromatin loop formation by cohesin.

The EMBO journal·2025
Same author

An extrinsic motor directs chromatin loop formation by cohesin.

The EMBO journal·2024
Same author

Telomere-to-telomere Schizosaccharomyces japonicus genome assembly reveals hitherto unknown genome features.

Yeast (Chichester, England)·2024
Same author

Mechanical disengagement of the cohesin ring.

Nature structural & molecular biology·2023
Same journal

Taphonomic analysis at Liang Bua reveals the behavioral and technological capabilities of <i>Homo floresiensis</i>.

Science advances·2026
Same journal

Targeting granule initiation and amyloplast structure to create giant starch granules in wheat.

Science advances·2026
Same journal

A meta-analysis of carbon losses and gains from tropical moist forest degradation and regeneration.

Science advances·2026
Same journal

Ancient DNA reveals elite dynastic rule among Iron Age Eurasian Steppe nomads.

Science advances·2026
Same journal

Targeting astrocytic Dp71 attenuates BBB disruption after traumatic brain injury through WTAP-associated m<sup>6</sup>A regulation of MMP2.

Science advances·2026
Same journal

Pancreatic α cells are required for nutrient homeostasis by regulating dynamic β cell networks in islets.

Science advances·2026
See all related articles

Related Experiment Video

Updated: Jan 11, 2026

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
11:50

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution

Published on: June 23, 2022

2.6K

Why is your separase such a big protease?

Céline Bouchoux1, Frank Uhlmann1

  • 1Chromosome Segregation Laboratory, The Francis Crick Institute, London NW1 1AT, UK.

Science Advances
|November 12, 2025
PubMed
Summary
This summary is machine-generated.

Researchers elucidated how the protease separase cleaves the chromosomal cohesin complex during cell division. This structural insight clarifies a fundamental step ensuring accurate chromosome segregation.

More Related Videos

In Vitro Cleavage Assays using Purified Recombinant Drosophila Caspases for Substrate Screening
08:16

In Vitro Cleavage Assays using Purified Recombinant Drosophila Caspases for Substrate Screening

Published on: October 6, 2022

1.9K
Online Size-exclusion and Ion-exchange Chromatography on a SAXS Beamline
11:09

Online Size-exclusion and Ion-exchange Chromatography on a SAXS Beamline

Published on: January 5, 2017

17.9K

Related Experiment Videos

Last Updated: Jan 11, 2026

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
11:50

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution

Published on: June 23, 2022

2.6K
In Vitro Cleavage Assays using Purified Recombinant Drosophila Caspases for Substrate Screening
08:16

In Vitro Cleavage Assays using Purified Recombinant Drosophila Caspases for Substrate Screening

Published on: October 6, 2022

1.9K
Online Size-exclusion and Ion-exchange Chromatography on a SAXS Beamline
11:09

Online Size-exclusion and Ion-exchange Chromatography on a SAXS Beamline

Published on: January 5, 2017

17.9K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Structural Biology

Background:

  • Cell division requires precise regulation of chromosome segregation.
  • The chromosomal cohesin complex holds sister chromatids together until anaphase.
  • The protease separase is responsible for cleaving cohesin to initiate sister chromatid separation.

Purpose of the Study:

  • To elucidate the structural mechanisms underlying the timely and specific cleavage of the chromosomal cohesin complex by separase.
  • To provide a molecular explanation for a fundamental event in cell division.

Main Methods:

  • X-ray crystallography
  • Cryo-electron microscopy
  • Biochemical assays

Main Results:

  • Detailed structural models of separase bound to cohesin were generated.
  • Key interactions mediating substrate recognition and cleavage were identified.
  • The structural basis for the specificity of cohesin cleavage was revealed.

Conclusions:

  • Structural insights explain how separase precisely targets and cleaves cohesin.
  • This mechanism is crucial for accurate chromosome segregation during cell division.
  • Understanding this process has implications for cell cycle regulation and cancer research.