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

Cohesins02:20

Cohesins

5.8K
Cohesin protein complexes are a molecular glue that holds two sister chromatids together. They play an important role both in mitosis and meiosis. In mitosis, all cohesin complexes present on the chromosomes are removed before the start of the anaphase stage.
Cohesin complexes in Meiotic Division
Meiosis involves two distinct rounds of chromosomal segregation and cell divisions— Meiosis I followed by Meiosis II – producing four daughter cells. Meiosis I includes the separation of...
5.8K
Cohesins02:20

Cohesins

2.4K
2.4K
Attachment of Sister Chromatids02:57

Attachment of Sister Chromatids

4.2K
As cells progress into mitosis, the nuclear envelope breaks down, and the condensed chromosomes are exposed to the array of bipolar microtubules of the mitotic spindle. The kinetochore, a large, disc-shaped protein complex, is present at the centromere region of the sister chromatids and acts as a binding site for the microtubules.  Usually, the plus-end of a single microtubule is embedded within the kinetochore. However, some kinetochores first establish lateral contact with the side-wall...
4.2K
Attachment of Sister Chromatids02:57

Attachment of Sister Chromatids

1.8K
1.8K
Separation of Sister Chromatids02:17

Separation of Sister Chromatids

4.7K
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...
4.7K
Separation of Sister Chromatids02:17

Separation of Sister Chromatids

2.5K
2.5K

You might also read

Related Articles

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

Sort by
Same author

Cancer-associated fibroblasts regulate DNA repair in pancreatic cancer through NDRG1-mediated R-loop processing.

Nature cell biology·2026
Same author

Human Peripheral Myelin Protein 2 and Charcot-Marie-Tooth Disease or Structural Missense Variants Show Different Binding to Myelin-Like Lipid Monolayers.

Chembiochem : a European journal of chemical biology·2026
Same author

Reversible RNA ADP-ribosylation on uracil bases.

Nucleic acids research·2026
Same author

Genetic commonalities between rare subtypes of ALS and CMT: insights into molecular mechanisms of neurodegeneration.

Amino acids·2026
Same author

Structural Analysis of Tilvestamab in Complex with AXL.

ACS omega·2026
Same author

The Chemical Composition and Baking Quality of Rye Flour from Grain with Organic Production.

Foods (Basel, Switzerland)·2026

Related Experiment Video

Updated: Mar 22, 2026

Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51
06:24

Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51

Published on: February 13, 2019

8.7K

Sister Chromatid Cohesion Establishment Factor ESCO1 Operates by Substrate-Assisted Catalysis.

Ekaterina Kouznetsova1, Takaharu Kanno2, Tobias Karlberg1

  • 1Structural Genomics Consortium and Department of Medical Biochemistry and Biophysics, Karolinska Institutet, 17177 Stockholm, Sweden.

Structure (London, England : 1993)
|April 27, 2016
PubMed
Summary

Sister chromatid cohesion establishment relies on SMC3 acetylation by ESCO1/Eco1 acetyltransferases. This study reveals ESCO1

More Related Videos

Author Spotlight: Investigating the Motion Dynamics of the Eukaryotic Replisome Components at the Single-Molecule Level
10:11

Author Spotlight: Investigating the Motion Dynamics of the Eukaryotic Replisome Components at the Single-Molecule Level

Published on: July 26, 2024

1.7K
OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

7.2K

Related Experiment Videos

Last Updated: Mar 22, 2026

Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51
06:24

Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51

Published on: February 13, 2019

8.7K
Author Spotlight: Investigating the Motion Dynamics of the Eukaryotic Replisome Components at the Single-Molecule Level
10:11

Author Spotlight: Investigating the Motion Dynamics of the Eukaryotic Replisome Components at the Single-Molecule Level

Published on: July 26, 2024

1.7K
OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

7.2K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Sister chromatid cohesion, mediated by the cohesin complex, is crucial for accurate chromosome segregation during cell division.
  • The acetylation of the SMC3 subunit by ESCO1/Eco1 homologs is essential for establishing cohesion, but the enzymatic mechanism remains elusive.

Purpose of the Study:

  • To elucidate the enzymatic mechanism of ESCO1 acetyltransferases in SMC3 acetylation.
  • To determine the structural basis for ESCO1's catalytic activity.

Main Methods:

  • Determined the crystal structure of the ESCO1 acetyltransferase domain in complex with acetyl-coenzyme A.
  • Utilized Small-Angle X-ray Scattering (SAXS) to assess ESCO1's quaternary structure in solution.
  • Performed site-directed mutagenesis on ESCO1 and budding yeast Smc3 to investigate catalytic mechanisms.

Main Results:

  • The crystal structure revealed an ESCO1 active site lacking a canonical catalytic base.
  • ESCO1 exists as a dimer in solution, as indicated by SAXS analysis.
  • Mutating a surface glutamate residue (E789) in ESCO1 significantly reduced its autoacetylation.
  • Mutating a conserved aspartate residue (D114) in budding yeast Smc3 prevented its in vivo acetylation.

Conclusions:

  • ESCO1 likely employs a substrate-assisted catalysis mechanism for SMC3 acetylation.
  • This mechanism is critical for controlling cohesion establishment and ensuring proper chromosome segregation.
  • The study provides a key mechanistic insight into the process of cohesion establishment.