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Author Spotlight: Advanced Single-Molecule Techniques for Investigating Telomeric Protein-DNA Interactions
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Structural and functional insights into yeast Tbf1 as an atypical telomeric repeat-binding factor.

Zhenfang Wu1, Xin Gu2, Lin Zha1

  • 1Key Laboratory of Systems Health Science of Zhejiang Province, School of Life Science, Hangzhou Institute for Advanced Study, University of Chinese Academy of Sciences, Hangzhou 310024, China.

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|April 27, 2024
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Telomeric repeat-binding factor 1 (Tbf1) in fission yeast binds telomeric DNA via its TRFH and Myb-L domains. Unlike other TRFs, Tbf1 lacks a shelterin docking motif, explaining its distinct functions.

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Area of Science:

  • Molecular biology
  • Structural biology
  • Genetics

Background:

  • Telomeric repeat-binding factor 1 (Tbf1) shares structural similarities with telomeric repeat-binding factors (TRFs) and influences telomere homeostasis and ribosome regulation.
  • The molecular mechanisms underlying Tbf1's distinct functions compared to other TRFs are not fully understood.

Purpose of the Study:

  • To elucidate the structural basis of Schizosaccharomyces pombe Tbf1 (spTbf1) function.
  • To investigate the role of spTbf1 domains in telomeric DNA binding and protein interactions.

Main Methods:

  • X-ray crystallography to determine the structures of spTbf1's TRF homology (TRFH) and Myb-L domains.
  • Biochemical assays to analyze spTbf1's DNA-binding capabilities and interactions.

Main Results:

  • The crystal structures of spTbf1 TRFH and Myb-L domains were determined.
  • TRFH-mediated homodimerization is crucial for spTbf1 stability.
  • spTbf1's TRFH domain lacks the conserved docking motif for shelterin complex interaction.
  • spTbf1 recognizes S. pombe telomeric double-stranded DNA through a coordinated effort of its TRFH, Myb-L domains, and a loop region.

Conclusions:

  • spTbf1 functions as an atypical telomeric repeat-binding factor in fungi.
  • The structural basis for spTbf1's unique role, distinct from shelterin components, is revealed.
  • These findings offer insights into the evolution of TRFH-containing telomeric proteins.