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A role for USP7 in DNA replication.

Madhav Jagannathan1, Tin Nguyen, David Gallo

  • 1Department of Molecular Genetics, University of Toronto, Toronto, Canada.

Molecular and Cellular Biology
|November 6, 2013
PubMed
Summary
This summary is machine-generated.

The ubiquitin-specific protease USP7, working with MCM-BP, helps unload minichromosome maintenance (MCM) complexes from chromatin after DNA replication. Its absence slows DNA synthesis by preventing MCM complex dissociation.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • The minichromosome maintenance (MCM) complex is crucial for DNA replication, loading onto chromatin post-mitosis and unloading post-S phase.
  • The unloading mechanism of MCM complexes from chromatin is not fully understood, with MCM binding protein (MCM-BP) implicated.

Purpose of the Study:

  • To investigate the role of USP7 in the unloading of MCM complexes from chromatin during DNA replication.
  • To elucidate the interaction between MCM-BP and USP7 and its functional significance.

Main Methods:

  • Biochemical assays and structural analyses to characterize the USP7-MCM-BP interaction.
  • USP7 knockout studies to assess effects on DNA replication.
  • Chromatin immunoprecipitation and protein level analysis to examine MCM protein dynamics.

Main Results:

  • MCM-BP directly interacts with USP7 on chromatin, tethering USP7 to MCM proteins via the (155)PSTS(158) sequence.
  • USP7 knockout leads to slowed progression through late S phase without affecting fork rate or origin usage.
  • Lack of USP7 causes increased MCM protein levels on chromatin due to impaired dissociation in mid- to late S phase.

Conclusions:

  • USP7, in conjunction with MCM-BP, plays a critical role in the unloading of MCM complexes from chromatin at the end of S phase.
  • USP7 is essential for efficient DNA replication progression by facilitating MCM complex removal from chromatin.