Biochemical characterization of the minichromosome maintenance protein from the archaeon Thermoplasma acidophilum

Extremophiles. 2009 Jan;13(1):81-8. doi: 10.1007/s00792-008-0198-y. Epub 2008 Nov 11.

Abstract

Minichromosome maintenance (MCM) proteins are thought to function as the replicative helicases in archaea. Studies have shown that the MCM complex from the thermoacidophilic euryarchaeon Thermoplasma acidophilum (TaMCM) has some properties not reported in other archaeal MCM helicases. Here, the biochemical properties of the TaMCM are studied. The protein binds single-stranded DNA, has DNA-dependent ATPase activity and ATP-dependent 3' --> 5' helicase activity. The optimal helicase conditions with regard to temperature, pH and salinity are similar to the intracellular conditions in T. acidophilum. It is also found that about 1,000 molecules of TaMCM are present per actively growing cell.

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Archaeal Proteins / metabolism*
  • Base Sequence
  • Chromosomes, Archaeal*
  • DNA Primers
  • DNA Replication
  • DNA, Single-Stranded / metabolism
  • Dimerization
  • Enzyme Activation
  • Fluorescence Polarization
  • Hydrogen-Ion Concentration
  • Temperature
  • Thermoplasma / enzymology
  • Thermoplasma / metabolism*
  • Two-Hybrid System Techniques

Substances

  • Archaeal Proteins
  • DNA Primers
  • DNA, Single-Stranded
  • Adenosine Triphosphatases