Divergent functions of multiple eukaryote-like Orc1/Cdc6 proteins on modulating the loading of the MCM helicase onto the origins of the hyperthermophilic archaeon Sulfolobus solfataricus P2

Biochem Biophys Res Commun. 2007 Sep 28;361(3):651-8. doi: 10.1016/j.bbrc.2007.07.073. Epub 2007 Jul 25.

Abstract

The Cdc6 protein has been suggested as a loader for the eukaryotic MCM helicase. Archaeal replication machinery represents a core version of that in eukaryotes. In the current work, three eukaryotic Orc1/Cdc6 homologs (SsoCdc6-1, -2, and -3) from crenarchaeon Sulfolobus solfataricus were shown to have totally different effects on the interactions with SsoMCM helicase. SsoCdc6-2 stimulates the binding of the SsoMCM onto the origin DNA, but SsoCdc6-1 and SsoCdc6-3 significantly inhibit the loading activities, and these inhibitive effects can not be reversed by the stimulation of SsoCdc6-2. Using pull-down assays, we showed that three SsoCdc6 proteins interacted physically with the SsoMCM. Furthermore, the C-terminal domains of SsoCdc6 proteins were shown to physically and functionally affect the interactions with SsoMCM. This is the first report on the divergent functions of multiple eukaryote-like Orc1/Cdc6 proteins on regulating the loading of the MCM helicase onto the origins in the archaeon.

MeSH terms

  • Archaeal Proteins / metabolism*
  • Base Sequence
  • Binding Sites
  • Cell Cycle Proteins / metabolism
  • DNA / metabolism
  • DNA Helicases / metabolism*
  • DNA Replication
  • Models, Genetic
  • Molecular Sequence Data
  • Origin Recognition Complex / metabolism*
  • Replication Origin*
  • Sulfolobus solfataricus / enzymology*
  • Sulfolobus solfataricus / genetics
  • Sulfolobus solfataricus / metabolism

Substances

  • Archaeal Proteins
  • Cell Cycle Proteins
  • Origin Recognition Complex
  • DNA
  • DNA Helicases