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

Jinyu Liu, Cheryl L. Smith, Deborah DeRyckere, Kristen DeAngelis, G. Steven Martin, James M. Berger

Research output: Contribution to journalArticlepeer-review

Abstract

Cdc6/Cdc18 is a conserved and essential component of prereplication complexes. The 2.0 Å crystal structure of an archaeal Cdc6 ortholog, in conjuction with a mutational analysis of the homologous Cdc18 protein from Schizosaccharomyces pombe, reveals novel aspects of Cdc6/Cdc18 function. Two domains of Cdc6 form an AAA+-type nucleotide binding fold that is observed bound to Mg·ADP. A third domain adopts a winged-helix fold similar to known DNA binding modules. Sequence comparisons show that the winged-helix domain is conserved in Orc1, and mutagenesis data demonstrate that this region of Cdc6/Cdc18 is required for function in vivo. Additional mutational analyses suggest that nucleotide binding and/or hydrolysis by Cdc6/Cdc18 is required not only for progression through S phase, but also for maintenance of checkpoint control during S phase.

Original languageEnglish (US)
Pages (from-to)637-648
Number of pages12
JournalMolecular cell
Volume6
Issue number3
DOIs
StatePublished - 2000

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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