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Condensins02:15

Condensins

Condensins are large protein complexes that use ATP to fuel the assembly of chromosomes during mitosis. They transform the tangled, shapeless mass of post-interphase DNA into individualized chromosomes by compacting, organizing, and segregating chromosomal DNA.
The plant and animal cells contain two types of condensin complexes—condensin I and condensin II. Both complexes have five subunits: two SMC (Structural Maintenance of Chromosomes) subunits, a kleisin subunit, and two HEAT-repeat...
Condensins02:15

Condensins

Condensins are large protein complexes that use ATP to fuel the assembly of chromosomes during mitosis. They transform the tangled, shapeless mass of post-interphase DNA into individualized chromosomes by compacting, organizing, and segregating chromosomal DNA.
The plant and animal cells contain two types of condensin complexes—condensin I and condensin II. Both complexes have five subunits: two SMC (Structural Maintenance of Chromosomes) subunits, a kleisin subunit, and two HEAT-repeat...
RNA Polymerase II Accessory Proteins02:36

RNA Polymerase II Accessory Proteins

Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
RNA Polymerase II Accessory Proteins02:36

RNA Polymerase II Accessory Proteins

Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
Cohesins02:20

Cohesins

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 homologous...
Eukaryotic Transcription Activators02:42

Eukaryotic Transcription Activators

Transcription activators are proteins that promote the transcription of genes from DNA to RNA. In most cases, these proteins contain two separate domains ‒ a domain that binds to DNA and a domain for activating transcription; however, in some cases, a single domain is responsible for both binding and activation of transcription, as seen in the glucocorticoid receptor and MyoD.
The binding domains are capable of recognizing and interacting with regulatory sequences on the DNA. These domains are...

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Related Experiment Video

Updated: Jun 13, 2026

Chemical Dimerization-Induced Protein Condensates on Telomeres
08:52

Chemical Dimerization-Induced Protein Condensates on Telomeres

Published on: April 12, 2021

Structural basis of condensin II activation.

Andrew Beel1, Pierre-Jean Mattei1, Dong-Hua Chen1

  • 1Department of Structural Biology, Stanford University, Stanford, CA 94305, USA.

Research Square
|June 12, 2026
PubMed
Summary

Human condensin II ( a protein complex essential for chromosome condensation) remains inactive until prophase. We discovered it forms a self-suppressed dimer in interphase, which is resolved by nucleotide binding and other factors.

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Related Experiment Videos

Last Updated: Jun 13, 2026

Chemical Dimerization-Induced Protein Condensates on Telomeres
08:52

Chemical Dimerization-Induced Protein Condensates on Telomeres

Published on: April 12, 2021

Single-Molecule Imaging of EWS-FLI1 Condensates Assembling on DNA
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Single-Molecule Imaging of EWS-FLI1 Condensates Assembling on DNA

Published on: September 8, 2021

Synthetic Condensates and Cell-Like Architectures from Amphiphilic DNA Nanostructures
08:02

Synthetic Condensates and Cell-Like Architectures from Amphiphilic DNA Nanostructures

Published on: May 31, 2024

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Structural Biology

Background:

  • Condensin II is crucial for chromosome condensation but its activity is cell-cycle regulated.
  • The mechanism keeping condensin II inactive during interphase is not well understood.

Purpose of the Study:

  • To elucidate the structural basis for condensin II autoinhibition during interphase.
  • To understand the regulation of condensin II activation.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine high-resolution structures.
  • Mass photometry to assess dimerization and complex formation.

Main Results:

  • Nucleotide-free human condensin II forms a reversible dimer at physiological ionic strength.
  • In the dimer, inhibitory elements (CAP-H2) are buried, and the CAP-D3 tail blocks key interactions.
  • Nucleotide binding promotes monomerization and structural rearrangements, but autoinhibition persists until further regulatory events.

Conclusions:

  • CAP-D3-dependent interactions mediate condensin II self-suppression.
  • This autoinhibitory mechanism explains the cell-cycle-dependent activation of condensin II.
  • The findings provide insights into the transition from an inactive to an active state, involving nucleotide binding and M18BP1 engagement.