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Papers In Press, published online ahead of print January 10, 2001
Molecular Microbiology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871
Corresponding Author: iwasaki{at}biken.osaka-u.ac.jp
Escherichia coli RuvC resolvase is a specific endonuclease that recognizes and cleaves Holliday junctions formed during homologous recombination and recombinational repair. This study examines the phenotype of RuvC mutants with amino acid substitutions at phenylalanine 69 (F69L, F69Y, F69W and F69A), a catalytically important residue that faces the catalytic center of the enzyme. F69Y, but not the other three mutants, almost fully complements the UV-sensitivity of a ruvC deletion strain, and substantially resolves synthetic Holliday junctions in vitro. In the presence of 100 mM NaCl, RuvC F69A and F69L are defective in junction binding, but F69Y and F69W retain near wild-type binding activity during a gel shift binding assay. KMnO4 was used to probe synthetic Holliday junction DNA in a complex with wild-type and mutant RuvC; F69A and F69L did not induce disruption of base-pairing at the crossover to the same extent as wild-type RuvC. Thus, the aromatic ring of F69 is involved in DNA binding, probably via a stacking interaction with a nucleotide base, and this interaction may induce a structural change in junction DNA that is required to form a catalytically competent complex.
J. Biol. Chem, 10.1074/jbc.M010138200
Submitted on November 7, 2000
Revised on January 5, 2001
Accepted on January 9, 2001
Evidence that phenylalanine 69 in Escherichia coli RuvC resolvase forms a stacking interaction during binding and destabilization of a holliday junction DNA substrate
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