Biochemical characterization of the minichromosome maintenance protein from the archaeon Thermoplasma acidophilum.
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.
Haugland
Gyri Teien
GT
Department of Biology, University of Bergen, PO Box 7800, 5020 Bergen, Norway. Gyri.Haugland@bio.uib.no
Rollor
Claire R
CR
Birkeland
Nils-Kåre
NK
Kelman
Zvi
Z
D000251:Adenosine Triphosphatases / Q000378:metabolism; D019843:Archaeal Proteins / Q000378:metabolism*; D001483:Base Sequence; D019847:Chromosomes, Archaeal; D017931:DNA Primers; D004261:DNA Replication; D004277:DNA, Single-Stranded / Q000378:metabolism; D019281:Dimerization; D004789:Enzyme Activation; D005454:Fluorescence Polarization; D006863:Hydrogen-Ion Concentration; D013696:Temperature; D013822:Thermoplasma / Q000201:enzymology / Q000378:metabolism*; D020798:Two-Hybrid System Techniques
D019843:Archaeal Proteins; D017931:DNA Primers; D004277:DNA, Single-Stranded; D000251:Adenosine Triphosphatases