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J. Biol. Chem., Vol. 277, Issue 31, 28019-28024, August 2, 2002
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and
From the Ludwig Institute for Cancer Research, Cancer Center and
Department of Medicine, University of California San Diego School
of Medicine, La Jolla, California 92093-0660
The MER3 protein of Saccharomyces
cerevisiae is required for crossover in meiosis and has
been suggested to act at the initiation of homologous pairing
and the resolution of Holliday junctions. The purified MER3 protein is
a DNA helicase that translocates along single-stranded DNA in the 3' to
5' direction displacing annealed DNA fragments. Here, MER3 was found to
be able to unwind various double-stranded DNA (dsDNA) substrates,
including a 30-bp dsDNA with a 20-nucleotide 3'-overhang, a 30-bp dsDNA
with a 20-nucleotide 5'-overhang, a 50-bp dsDNA with blunt ends, and a
Holliday junction with 25-bp arms, each of which had a blunt end.
Efficient unwinding of the 3'-overhang substrate appeared to initiate
by the binding of MER3 to the 3' single-stranded tail in a reaction
that required six or more unpaired bases. Unwinding of the blunt end
and 5'-overhang substrates appeared to initiate at the blunt ends of
these substrates. Unwinding of the Holliday junction was more efficient
than the unwinding of the blunt and 5'-overhang substrates and was
influenced by Mg2+ concentrations that cause changes in the
structure of the junction. Possible roles for Holliday junction
unwinding in meiotic crossover are discussed.
Supported by the Japan Society for the Promotion of Science and
Human Frontier Science Program. Present address: Dept. of Biology,
Osaka University Graduate School of Science, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.
§
To whom correspondence should be addressed: Ludwig Inst. 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.
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