Nucleic Acids Research Advance Access published online on November 15, 2006
Nucleic Acids Research, doi:10.1093/nar/gkl864
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Nucleic Acid Enzymes |
Stimulation of MCM helicase activity by a Cdc6 protein in the archaeon Thermoplasma acidophilum
Department of Biology, University of Bergen PO Box 7800, N-5020 Bergen, Norway 1 University of Maryland Biotechnology Institute, Center for Advanced Research in Biotechnology 9600 Gudelsky Drive, Rockville, MD 20850, USA
*To whom correspondence should be addressed. Tel: +1 240 314 6294; Fax: +1 240 314 6255; Email: kelman{at}umbi.umd.edu
Received July 20, 2006. Revised October 2, 2006. Accepted October 4, 2006.
Replicative DNA helicases are ring-shaped hexamers that play an essential role in chromosomal DNA replication. They unwind the two strands of the duplex DNA and provide the single-stranded (ss) DNA substrate for the polymerase. The minichromosome maintenance (MCM) proteins are thought to function as the replicative helicases in eukarya and archaea. The proteins of only a few archaeal organisms have been studied and revealed that although all have similar amino acid sequences and overall structures they differ in their biochemical properties. In this report the biochemical properties of the MCM protein from the archaeon Thermoplasma acidophilum is described. The enzyme has weak helicase activity on a substrate containing only a 3'-ssDNA overhang region and the protein requires a forked DNA structure for efficient helicase activity. It was also found that the helicase activity is stimulated by one of the two T.acidophilum Cdc6 homologues. This is an interesting observation as it is in sharp contrast to observations made with MCM and Cdc6 homologues from other archaea in which the helicase activity is inhibited when bound to Cdc6.
The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors
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