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Structural Basis for Shelterin Bridge Assembly.

Jin-Kwang Kim1, Jinqiang Liu1, Xichan Hu1

  • 1Department of Biological Chemistry, School of Medicine, University of California, Irvine, Irvine, CA 92697-1700, USA.

Molecular Cell
|November 18, 2017
PubMed
Summary

Shelterin complex assembly is hierarchical, with Tpz1 binding Poz1, which then recruits Rap1. This process, crucial for telomere maintenance, is conserved across species.

Keywords:
X-ray crystallographyallosteric structural changeschromosomecooperativitygenome instabilityhierarchical assemblyprotein interactionsshelterintelomerasetelomeres

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Genetics

Background:

  • Telomeres protect chromosome ends during cell division.
  • The shelterin complex regulates telomere length and stability.
  • Fission yeast and human shelterin complexes share homologous proteins.

Purpose of the Study:

  • To elucidate the structural basis of fission yeast shelterin complex assembly.
  • To investigate the mechanism of shelterin bridge formation.
  • To determine the evolutionary conservation of shelterin assembly dynamics.

Main Methods:

  • X-ray crystallography of the Tpz1-Poz1-Rap1 complex.
  • Biochemical analyses of protein-protein interactions.
  • Site-directed mutagenesis to study the 'conformational trigger' in Poz1.

Main Results:

  • Determined the crystal structure of the fission yeast Tpz1-Poz1-Rap1 complex.
  • Shelterin bridge assembly is a hierarchical, allosteric process.
  • Mutating the Poz1 'conformational trigger' causes unregulated telomere lengthening.
  • Human shelterin components TPP1-TIN2-TRF2 also assemble hierarchically.

Conclusions:

  • Shelterin complex assembly is a cooperative and hierarchical process.
  • This assembly mechanism is conserved between fission yeast and humans.
  • Dysregulation of this cooperative assembly leads to uncontrolled telomere elongation.