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Cohesins02:20

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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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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.
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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Protein Folding01:25

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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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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For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
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Genome folding by cohesin.

Shutao Qi1, Zhubing Shi2, Hongtao Yu1

  • 1School of Life Sciences, Westlake University, Hangzhou, Zhejiang, China; Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, China; New Cornerstone Science Laboratory, Westlake University, Hangzhou, Zhejiang, China.

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The cohesin complex, an ATPase machine, drives genome folding by extruding DNA loops. This process organizes chromosomes and regulates gene transcription by controlling enhancer-promoter interactions.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Cell Biology

Background:

  • Eukaryotic chromosomes require hierarchical folding for nuclear organization.
  • This 3D genome structure is crucial for DNA replication and gene transcription.
  • The cohesin complex is a key ATPase machine involved in genome folding.

Purpose of the Study:

  • To review the current understanding of cohesin-mediated genome folding.
  • To summarize evidence for cohesin's role in loop extrusion.
  • To discuss cohesin conformations, regulation, and propose a new model.

Main Methods:

  • Literature review of cohesin function in genome organization.
  • Analysis of evidence supporting the loop extrusion model.
  • Discussion of regulatory factors and cohesin conformations.

Main Results:

  • Cohesin acts as a major driver of genome folding.
  • Evidence supports cohesin's role in forming chromatin loops and TADs via loop extrusion.
  • Cohesin conformation and binding factors regulate this process.

Conclusions:

  • Cohesin-mediated loop extrusion is a fundamental mechanism for 3D genome organization.
  • This process impacts gene transcription by modulating enhancer-promoter contacts.
  • A dimeric inchworm model is proposed for cohesin's loop extrusion activity.