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Papers In Press, published online ahead of print September 25, 2000
Department of Molecular Biology, Biomolecular Engineering Resaerch Institute, Suita, Osaka 565-0874
Corresponding Author: ishino{at}beri.co.jp
The Hjc resolvase of Pyrococcus furiosus is the first Holliday junction resolvase discovered in Archaea. Although it shares certain biochemical properties with other non-archaeal junction resolvases, no amino acid sequence similarity to them is identified. To investigate the structure-function relationship of this new Holliday junction resolvase, we constructed a series of mutant hjc genes by site-directed mutagenesis targeted at the residues conserved among the archaeal orthologs. The products of these mutant genes were purified to homogeneity. By analyzing the abilities of the mutant proteins to bind and cleave synthetic Holliday junctions, one acidic residue, Glu9, and two basic residues, Arg10 and Arg25, were found to play critical roles in the catalysis of this enzyme, in addition to the three conserved residues, Asp33, Glu46, and Lys48, which are also conserved in the motif found in the type II restriction endonuclease family proteins. Two aromatic residues, Phe68 and Phe72, are important for the formation of the homodimer, probably by the hydrophobic interactions. The results of these studies will contribute to the understanding of the structure-function relationships of the archaeal Holliday junction resolvase, and furthermore, to the understanding of the universality and diversity of the Holliday junction cleavage reaction.
J. Biol. Chem, 10.1074/jbc.M006294200
Submitted on July 17, 2000
Revised on September 20, 2000
Accepted on September 24, 2000
Mutational analysis of the Pyrococcus furiosus Holliday junction resolvase Hjc revealed functionally important residues for dimer formation, junction DNA binding and cleavage activities
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