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

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TitleBiochemical characterization of the minichromosome maintenance protein from the archaeon Thermoplasma acidophilum.
Publication TypeJournal Article
Year of Publication2009
AuthorsHaugland, GTeien, Rollor, CR, Birkeland, N-K, Kelman, Z
JournalExtremophiles
Volume13
Issue1
Pagination81-8
Date Published2009 Jan
ISSN1433-4909
KeywordsAdenosine Triphosphatases, Archaeal Proteins, Base Sequence, Chromosomes, Archaeal, Dimerization, DNA Primers, DNA Replication, DNA, Single-Stranded, Enzyme Activation, Fluorescence Polarization, Hydrogen-Ion Concentration, Temperature, Thermoplasma, Two-Hybrid System Techniques
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.

DOI10.1007/s00792-008-0198-y
Alternate JournalExtremophiles
PubMed ID19002376