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Spring loading a pre-cleavage intermediate for hairpin telomere formation.

Danica Lucyshyn1, Shu Hui Huang1, Kerri Kobryn2

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Borrelia telomere resolvase (ResT) unwinds DNA, a crucial cold-sensitive step for forming hairpin telomeres. This process involves cooperation between ResT

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Borrelia species possess linear chromosomes with unique hairpin telomeres.
  • Telomere resolution, mediated by the Borrelia telomere resolvase (ResT), is essential for replicating these linear replicons.
  • ResT shares mechanistic similarities with type IB topoisomerases, involving DNA cleavage and rejoining.

Purpose of the Study:

  • To elucidate the mechanism of telomere resolution by Borrelia telomere resolvase (ResT).
  • To investigate the role of DNA unwinding as a key step in telomere resolution.
  • To understand the interplay between ResT's domains in promoting hairpin telomere formation.

Main Methods:

  • Analysis of ResT mutants with altered DNA binding and catalytic activities.
  • Utilized substrate modifications to mimic DNA unwinding between cleavage sites.
  • Investigated the cold-sensitive nature of the DNA unwinding step in telomere resolution.

Main Results:

  • DNA unwinding between scissile phosphates is identified as a critical, cold-sensitive step in telomere resolution.
  • Cooperation between ResT's hairpin-binding module and catalytic domain is essential for forming an underwound pre-cleavage intermediate.
  • The pre-cleavage intermediate facilitates strand ejection, favoring forward reaction and reversible hairpin capture.

Conclusions:

  • ResT-mediated telomere resolution involves a crucial DNA unwinding step regulated by domain cooperation.
  • The reaction mechanism favors hairpin formation over strand resealing, ensuring efficient telomere maintenance.
  • Understanding this process provides insights into DNA replication and repair mechanisms in Borrelia.