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Volume 2010, Article ID 505693, 8 pages
Research Article

Different Residues on the Surface of the Methanothermobacter thermautotrophicus MCM Helicase Interact with Single- and Double-Stranded DNA

1Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, 9600 Gudelsky Drive, Rockville, MD 20850, USA
2Laboratory of Viral Diseases, NIAID, NIH, 4 Center Drive, Bethesda, MD 20892, USA
3Laboratory of Molecular Genetics, National Institute of Environmental Health Sciences, 111 TW Alexander Drive, Research Triangle Park, NC 27709, USA
4Department of Cell Biology and Molecular Genetics, Institute for Bioscience and Biotechnology Research, University of Maryland, 9600 Gudelsky Drive, Rockville, MD 20850, USA

Received 5 August 2010; Accepted 16 October 2010

Academic Editor: Y. Ishino

Copyright © 2010 Nozomi Sakakibara et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Supplementary Material

Supplementary Table 1 shows the oligonucleotides used to generate the mutant proteins using PCR-mediated mutagenesis.

Supplementary Figure 1 shows the effect of the two M. thermautotrophicus Cdc6 proteins on the helicase activity of the wild‐type and mutant MCM proteins.

  1. Supplementary Table 1
  2. Supplementary Figure 1