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Papers In Press, published online ahead of print May 25, 2001
J. Biol. Chem, 10.1074/jbc.M104003200
Submitted on May 3, 2001
Revised on May 25, 2001
Accepted on May 24, 2001
Ludwig Institute for Cancer Research, La Jolla, CA 92093-0660
Corresponding Author: rkolodner{at}ucsd.edu
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 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 per minute in the presence of either DNA. MER3 was able to efficiently displace relatively long 631-nt fragments from single-stranded circular DNA only in the presence of the S. cerevisiae single strand DNA binding protein Replication Protein A (RPA). 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.
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