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Direct Restart of a Replication Fork Stalled by a Head-On RNA Polymerase
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Mitotic entry drives replisome disassembly at stalled replication forks.

Yoshitami Hashimoto1, Hirofumi Tanaka1

  • 1School of Life Sciences, Tokyo University of Pharmacy and Life Sciences, 1432-1 Horinouchi, Hachioji, Tokyo, 192-0392, Japan.

Biochemical and Biophysical Research Communications
|October 21, 2018
PubMed
Summary

A new pathway disassembles the eukaryotic replisome at stalled replication forks entering M-phase. This process relies on M-CDK activity and specific ubiquitylation, distinct from known mechanisms.

Keywords:
CDKCMG complexReplisomeUbiquitylationXenopus egg extractp97/VCP/Cdc48

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Eukaryotic replisome disassembly at replication termination involves CRL-dependent ubiquitylation of Mcm7 and p97.
  • Mechanisms for replisome disassembly at stalled or collapsed forks under stress are not well understood.

Purpose of the Study:

  • To elucidate the novel mechanism of stepwise replisome disassembly at stalled replication forks that persist into M-phase.

Main Methods:

  • Utilized Xenopus egg extracts to study replisome disassembly.
  • Investigated pathways dependent on M-CDK activity and K48/K63-linked poly-ubiquitylation.

Main Results:

  • Discovered a novel pathway for replisome disassembly at stalled forks entering M-phase.
  • This pathway is dependent on M-CDK and specific ubiquitylation, independent of CRL and p97.
  • The pathway could not disassemble converged replisomes with pre-ubiquitylated Mcm7 without p97.

Conclusions:

  • A distinct pathway mediates replisome disassembly when stalled forks persist into M-phase.
  • This mechanism differs from known CRL- and p97-dependent pathways.