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Related Concept Videos

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Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3...
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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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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.
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Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins
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Structural basis of centromeric cohesion protection.

Alberto García-Nieto1, Amrita Patel2, Yan Li3

  • 1Division of Cell Biology, The Netherlands Cancer Institute, Amsterdam, the Netherlands.

Nature Structural & Molecular Biology
|April 20, 2023
PubMed
Summary
This summary is machine-generated.

Shugoshin 1 (SGO1) protects centromeric cohesin during mitosis by binding to the cohesin complex. This interaction ensures proper chromosome segregation and karyotype stability.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Cohesin establishes sister chromatid cohesion, crucial for accurate chromosome segregation during mitosis.
  • Centromeric cohesin is protected by Shugoshin 1 (SGO1) to withstand spindle forces until bipolar attachment.
  • The release of cohesin from chromosome arms occurs early in mitosis, while centromeric cohesin is protected.

Purpose of the Study:

  • To determine the structural basis of SGO1 interaction with the cohesin complex.
  • To elucidate the mechanism by which SGO1 protects centromeric cohesin.
  • To understand the role of SGO1-cohesin binding in faithful chromosome segregation.

Main Methods:

  • X-ray crystallography was used to determine the structure of human SGO1 bound to cohesin.
  • Biochemical assays were employed to analyze the binding interface and functional consequences.

Main Results:

  • The crystal structure reveals SGO1 binding to a composite interface on cohesin, involving SA2 and SCC1RAD21 subunits.
  • SGO1 shares this binding interface with CTCF, suggesting a common regulatory principle for cohesin.
  • SGO1 binding is essential for its centromeric localization and protects cohesin from WAPL-mediated release.

Conclusions:

  • SGO1-cohesin interaction is vital for maintaining centromeric cohesion until microtubule-kinetochore attachments are established.
  • This interaction is critical for ensuring faithful chromosome segregation and maintaining karyotype stability.
  • The shared binding interface highlights a conserved mechanism for regulating cohesin function by distinct chromosomal proteins.