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J. Biol. Chem., Vol. 282, Issue 7, 4908-4915, February 16, 2007

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Archaeal Minichromosome Maintenance (MCM) Helicase Can Unwind DNA Bound by Archaeal Histones and Transcription Factors^*

Jae-Ho Shin, Thomas J. Santangelo¹, Yunwei Xie², John N. Reeve, and Zvi Kelman³

From the Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850 and the Department of Microbiology, Ohio State University, Columbus, Ohio 43210

Protein-DNA complexes must be disassembled to facilitate DNA replication. Replication forks contain a helicase that unwinds the duplex DNA at the front of the fork. The minichromosome maintenance helicase from the archaeon Methanothermobacter thermautotrophicus required only ATP to unwind DNA bound into complexes by the M. thermautotrophicus archaeal histone HMtA2, transcription repressor TrpY, or into a transcription pre-initiation complex by M. thermautotrophicus TATA-box-binding protein, transcription factor B, and RNA polymerase. In contrast, the minichromosome maintenance helicase was unable to unwind DNA bound by this archaeal RNA polymerase in a stalled transcript-elongating complex.

Received for publication, July 18, 2006 , and in revised form, November 22, 2006.

^* This work was supported in part by Research Scholar Grant RSG-04-050-01-GMC from the American Cancer Society (to Z. K.) for research at the Center for Advanced Research in Biotechnology and by Grants DE-FG02-87ER13731 and GM53185 (to J. N. R.) from the Department of Energy and the National Institutes of Health, respectively, for research at the Ohio State University. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Supported by National Institutes of Health postdoctoral fellowship (GM073336-01).

² Present address: Lombardi Cancer Center, Georgetown University, Washington, D. C. 20057.

³ To whom correspondence should be addressed: Univ. of Maryland Biotechnology Inst., Center for Advanced Research in Biotechnology, 9600 Gudelsky Dr., Rockville, MD 20850. Tel.: 240-314-6294; Fax: 240-314-6245; E-mail: kelman{at}umbi.umd.edu.

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				J.-H. Shin, G. Y. Heo, and Z. Kelman The Methanothermobacter thermautotrophicus Cdc6-2 Protein, the Putative Helicase Loader, Dissociates the Minichromosome Maintenance Helicase J. Bacteriol., June 1, 2008; 190(11): 4091 - 4094. [Abstract] [Full Text] [PDF]

				N. Sakakibara, R. Kasiviswanathan, E. Melamud, M. Han, F. P. Schwarz, and Z. Kelman Coupling of DNA binding and helicase activity is mediated by a conserved loop in the MCM protein Nucleic Acids Res., March 27, 2008; 36(4): 1309 - 1320. [Abstract] [Full Text] [PDF]