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Originally published In Press as doi:10.1074/jbc.M104003200 on May 25, 2001

J. Biol. Chem., Vol. 276, Issue 34, 31487-31493, August 24, 2001
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The MER3 Helicase Involved in Meiotic Crossing Over Is Stimulated by Single-stranded DNA-binding Proteins and Unwinds DNA in the 3' to 5' Direction*

Takuro NakagawaDagger , Hernan Flores-Rozas§, and Richard D. Kolodner

From the Cancer Center, Department of Medicine, and Ludwig Institute for Cancer Research, University of California San Diego School of Medicine, La Jolla, California 92093-0660

The meiosis-specific MER3 protein of Saccharomyces cerevisiae is required for crossing over, which ensures faithful segregation of homologous chromosomes at the first meiotic division. The predicted sequence of the MER3 protein contains the seven motifs characteristic of the DExH-box type of DNA/RNA helicases. The purified MER3 protein is a DNA helicase, which can displace a 50-nucleotide fragment annealed to a single-stranded circular DNA. MER3 was found to have ATPase activity, which was stimulated either by single- or double-stranded DNA. The turnover rate, kcat, of ATP hydrolysis was ~500/min in the presence of either DNA. MER3 was able to efficiently displace relatively long 631-nucleotide fragments from single-stranded circular DNA only in the presence of the S. cerevisiae single-stranded DNA-binding protein, RPA (replication protein A). It appears that RPA inhibits re-annealing of the single-stranded products of the MER3 helicase. The MER3 helicase was found to unwind DNA in the 3' to 5' direction relative to single-stranded regions in the DNA substrates. Possible roles for the MER3 helicase in meiotic crossing over are discussed.

* This work was supported by National Institutes of Health Grant GM26017 (to R. D. K.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Supported by the Human Frontier Science Program. Present address: Dept. of Biology, Osaka University Graduate School of Science, Machikaneyama, Toyonaka, Osaka 560-0043, Japan.

§ Supported by the Jane Coffin Childs Memorial Fund for Medical Research.

To whom correspondence should be addressed: Ludwig Institute for Cancer Research, University of California San Diego School of Medicine, CMME 3080, 9500 Gilman Dr., La Jolla, CA 92093-0660. Tel.: 858-534-7804; Fax: 858-534-7750; E-mail: rkolodner@ucsd.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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