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Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control.

J Liu1, C L Smith, D DeRyckere

  • 1Department of Molecular and Cell Biology, University of California, Berkeley 94720, USA.

Molecular Cell
|October 13, 2000
PubMed
Summary
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The study reveals the structure and function of Cdc6/Cdc18, an essential protein for DNA replication. Its winged-helix domain is crucial for DNA binding and cell cycle control, highlighting its role in S phase progression and checkpoint maintenance.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Structural Biology

Background:

  • Cdc6/Cdc18 is a conserved protein essential for DNA replication initiation.
  • Prereplication complexes require Cdc6/Cdc18 for proper function.

Purpose of the Study:

  • To elucidate the structural basis of Cdc6/Cdc18 function.
  • To investigate the role of specific domains in Cdc6/Cdc18 activity and regulation.

Main Methods:

  • X-ray crystallography of an archaeal Cdc6 ortholog.
  • Site-directed mutagenesis of the homologous Cdc18 protein in Schizosaccharomyces pombe.
  • Sequence comparisons with related proteins.

Main Results:

  • The crystal structure revealed two domains forming an AAA+-type nucleotide-binding fold and a third winged-helix domain.

Related Experiment Videos

  • The winged-helix domain is conserved in Orc1 and is essential for Cdc6/Cdc18 function in vivo.
  • Nucleotide binding/hydrolysis is critical for S phase progression and checkpoint control.

    • Conclusions:

    • Cdc6/Cdc18 possesses a unique structural organization with distinct functional domains.
    • The winged-helix domain plays a key role in DNA interaction and cellular processes.
    • Cdc6/Cdc18 is vital for both DNA replication and cell cycle checkpoint mechanisms.