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Nucleic Acids Research Advance Access originally published online on August 30, 2008
Nucleic Acids Research 2008 36(17):5602-5609; doi:10.1093/nar/gkn548
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Nucleic Acids Research, 2008, Vol. 36, No. 17 5602-5609
© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Nucleic Acid Enzymes

Thermoplasma acidophilum Cdc6 protein stimulates MCM helicase activity by regulating its ATPase activity

Gyri Teien Haugland1, Nozomi Sakakibara2, Angel L. Pey3, Claire R. Rollor2, Nils-Kåre Birkeland1 and Zvi Kelman2,*

1Department of Biology, University of Bergen, N-5020 Bergen, Norway, 2University of Maryland Biotechnology Institute, Center for Advanced Research in Biotechnology, 9600 Gudelsky Drive, Rockville, MD 20850, USA and 3Department of Biomedicine, University of Bergen, Jonas Lies Vei 91, N-5009 Bergen, Norway

*To whom correspondence should be addressed. Tel: +1 240 314 6294; Fax: +1 240 314 6255; Email: kelman{at}umbi.umd.edu

Received May 27, 2008. Revised July 7, 2008. Accepted August 12, 2008.

The minichromosome maintenance (MCM) proteins are thought to function as the replicative helicases in archaea. In most archaeal species studied, the interaction between MCM and the initiator protein, Cdc6, inhibits helicase activity. To date, the only exception is the helicase and Cdc6 proteins from the archaeon Thermoplasma acidophilum. It was previously shown that when the Cdc6 protein interacts with MCM it substantially stimulates helicase activity. It is shown here that the mechanism by which the Cdc6 protein stimulates helicase activity is by stimulating the ATPase activity of MCM. Also, through the use of site-specific substitutions, and truncated and chimeric proteins, it was shown that an intact Cdc6 protein is required for this stimulation. ATP binding and hydrolysis by the Cdc6 protein is not needed for the stimulation. The data suggest that binding of Cdc6 protein to MCM protein changes the structure of the helicase, enhancing the catalytic hydrolysis of ATP and helicase activity.


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