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M403202200v1
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Papers In Press, published online ahead of print April 20, 2004
J. Biol. Chem, 10.1074/jbc.M403202200
Submitted on March 22, 2004
Revised on April 20, 2004
Accepted on April 20, 2004

Biochemical characterization of the methanothermobacter thermautotrophicus minichromosome maintenance (MCM) helicase N-terminal domains

Rajesh Kasiviswanathan, Jae-Ho Shin, Eugene Melamud, and Zvi Kelman

Center for Advanced Research in Biotechnology, Rockville, MD 20850

Corresponding Author: kelman{at}umbi.umd.edu

Minichromosome maintenance (MCM) helicases are ring-shaped complexes that play an essential role in archaeal and eukaryal DNA replication by separating the two strands of chromosomal DNA to provide the single-stranded substrate for the replicative polymerases. For the archaeal protein it was shown that the N-terminal portion of the protein, which is composed of domains A, B and C, is involved in multimer formation, single-stranded DNA binding, and may also play a role in regulating the helicase activity. Here, a detailed biochemical characterization of the N-terminal region of the Methanothermobacter thermautotrophicus MCM helicase is described. Using biochemical and biophysical analyses it is shown that domain C of the N-terminal portion, located adjacent to the helicase catalytic domains, is required for protein multimerization, and that domain B is the main contact region with ssDNA. It is also shown that while oligomerization is not essential for ssDNA binding and ATPase activity, the presence of domain C is essential for helicase activity.


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