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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.
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Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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Each human somatic cell contains 6 billion base-pairs of DNA. Each base-pair is 0.34 nm long, which means that each diploid cell contains a staggering 2 meters of DNA. How is such a long DNA strand packed inside a nucleus measuring only 10 - 20 microns in diameter? 
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CTCF and cohesin regulate chromatin loop stability with distinct dynamics.

Anders S Hansen1,2,3,4, Iryna Pustova1,2,3,4, Claudia Cattoglio1,2,3,4

  • 1Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.

Elife
|May 4, 2017
PubMed
Summary
This summary is machine-generated.

Mammalian genome folding relies on CTCF and cohesin. These proteins form a dynamic complex, suggesting that chromatin loops are not stable but frequently break and reform.

Keywords:
CTCFbiophysicschromosomescohesingenesgenome organizationhumanimagingmousesingle-moleculestructural biology

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Area of Science:

  • Genomics
  • Molecular Biology
  • Epigenetics

Background:

  • Mammalian genome folding into spatial domains is crucial for gene regulation.
  • The insulator protein CTCF and cohesin are known to form loop structures that define these domains.
  • These loop structures have been widely considered to be stable.

Purpose of the Study:

  • To investigate the dynamic nature of the complex formed by CTCF and cohesin.
  • To determine the residence times and binding/unbinding dynamics of CTCF and cohesin on chromatin.
  • To understand the implications of these dynamics for chromatin loop stability.

Main Methods:

  • Genomic and biochemical approaches were used to study CTCF and cohesin interactions.
  • Single-molecule imaging was employed to measure the dynamic binding of CTCF and cohesin to chromatin.
  • Residence times and search processes for both proteins were quantified.

Main Results:

  • CTCF and cohesin co-occupy the same genomic sites and interact biochemically.
  • CTCF exhibits significantly shorter chromatin residence times (~1-2 min) compared to cohesin (~22 min).
  • CTCF rapidly rebinds to cognate sites after unbinding, while cohesin has a longer search process (~33 min).

Conclusions:

  • CTCF and cohesin form a 'dynamic complex' characterized by rapid exchange, not a stable one.
  • The dynamic nature of this complex suggests that chromatin loops are transient structures.
  • Chromatin loops likely break and reform frequently throughout the cell cycle, impacting gene regulation.