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Related Experiment Videos

Mammalian Mcm2/4/6/7 complex forms a toroidal structure.

Norikazu Yabuta1, Naoko Kajimura, Kouta Mayanagi

  • 1Department of Molecular Genetics, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita, Osaka 565-0871, Japan.

Genes to Cells : Devoted to Molecular & Cellular Mechanisms
|April 16, 2003
PubMed
Summary

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The Mcm2-7 protein complex, crucial for DNA replication, forms a toroidal structure. This distinct toroidal shape differs from the Mcm4/6/7 hexamer, providing new insights into replication machinery.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • The Mcm2-7 protein family is essential for DNA replication.
  • Mcm proteins assemble into Mcm4/6/7 and Mcm2/4/6/7 complexes.
  • The precise structures of these complexes were previously unknown.

Purpose of the Study:

  • To determine the structural organization of the human Mcm2/4/6/7 tetramer.
  • To compare the structure of the Mcm2/4/6/7 tetramer with the Mcm4/6/7 hexamer.

Main Methods:

  • Single-particle electron microscopy and image analysis were employed.
  • Comparative structural analysis with mouse Mcm2/4/6/7 tetramer.
  • Biochemical assays including GST-pull down and two-hybrid experiments.

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Main Results:

  • The human Mcm2/4/6/7 tetramer adopts a toroidal structure with a central cavity (3-4 nm diameter).
  • A predominant averaged image revealed a toroid with four bulges, one larger than the others.
  • This structure closely resembles the mouse Mcm2/4/6/7 tetramer and differs from the Mcm4/6/7 hexamer.

Conclusions:

  • The Mcm2/4/6/7 tetramer forms a distinct toroidal structure.
  • This structure is differentiated in size and shape from the Mcm4/6/7 hexamer.
  • A Mcm6-Mcm6 hinge is suggested to be involved in Mcm7/4/6/6/4/7 heterohexamer formation.