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Cdt1 stabilizes an open MCM ring for helicase loading.

Jordi Frigola1, Jun He1,2, Kerstin Kinkelin1

  • 1Chromosome Replication Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.

Nature Communications
|June 24, 2017
PubMed
Summary
This summary is machine-generated.

Cdt1 protein acts as a brace to open the MCM helicase motor for DNA loading. This interaction inhibits ATPase activity until ORC-Cdc6 triggers hydrolysis, promoting DNA replication initiation.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • The MCM complex forms the core of the eukaryotic replicative helicase, essential for DNA replication.
  • ORC, Cdc6, and Cdt1 are key regulators involved in loading the MCM complex onto DNA at replication origins.

Purpose of the Study:

  • To elucidate the structural and functional role of Cdt1 in the MCM loading process.
  • To understand how Cdt1 interacts with MCM subunits and influences its activity.

Main Methods:

  • X-ray crystallography was used to determine the structure of Cdt1 and its domains.
  • Single-particle electron microscopy (cryo-EM) was employed to generate 3D models of MCM-Cdt1 complexes.
  • Biochemical assays were performed to assess MCM ATPase activity.

Main Results:

  • Cdt1 interacts with MCM subunits Mcm2, Mcm4, and Mcm6, destabilizing the Mcm2-5 interface.
  • Cdt1 inhibits the ATPase activity of the MCM complex.
  • Structural analysis revealed Cdt1 stabilizes MCM in an open conformation, facilitating DNA entry.
  • Cdt1 possesses winged-helix domains and a catalytically inactive N-terminal domain crucial for MCM loading.

Conclusions:

  • Cdt1 acts as a molecular brace, holding the MCM helicase open for DNA binding and ATP binding.
  • The interaction between Cdt1 and MCM is crucial for regulated initiation of DNA replication.
  • ORC-Cdc6 triggers MCM ATP hydrolysis, leading to Cdt1 release and MCM ring closure, initiating replication.