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Archaeal MCM has separable processivity, substrate choice and helicase domains

Elizabeth R Barry1, Adam T McGeoch, Zvi Kelman

  • 1MRC Cancer Cell Unit, Hutchison MRC Research Centre, Hills Road, Cambridge, CB2 2XZ, UK.

Nucleic Acids Research
|January 30, 2007
PubMed

Insights

The mini-chromosome maintenance (MCM) complex

Area of Science:

  • Molecular biology
  • Biochemistry
  • Structural biology

Background:

  • The mini-chromosome maintenance (MCM) complex is a key replicative helicase in archaea and eukaryotes.
  • Understanding MCM complex function requires dissecting the roles of its structural modules.

Purpose of the Study:

  • To functionally dissect the roles of the three principal structural modules of the homomultimeric MCM complex from Sulfolobus solfataricus.
  • To analyze the isolated central AAA+ domain for its intrinsic enzymatic activities.

Main Methods:

  • Functional dissection of MCM structural modules.
  • In vitro biochemical assays including ATPase and helicase activity measurements.
  • Reconstitution experiments with isolated MCM domains.

Main Results:

  • The central AAA+ domain possesses intrinsic ATPase and helicase activity, representing the minimal helicase domain.
  • The N-terminal half stimulates helicase activity and influences processivity and substrate selection.
  • The C-terminal helix-turn-helix domain negatively impacts helicase activity.

Conclusions:

  • The AAA+ domain is the minimal catalytic unit for MCM helicase activity.
  • Inter-domain communication within the MCM complex regulates its function.
  • Distinct structural modules contribute to the regulation of helicase activity and substrate specificity.

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