title: Conserved sequence preference in DNA binding among recombination proteins: an effect of ssDNA secondary structure.
abstract: Repetitive sequences have been proposed to be recombinogenic elements in eukaryotic chromosomes. We tested whether dinucleotide repeats sequences are preferential sites for recombination because of their high affinity for recombination enzymes. We compared the kinetics of the binding of the scRad51, hsRad51 and ecRecA proteins to oligonucleotides with repeats of dinucleotides GT, CA, CT, GA, GC or AT. Since secondary structures in single-stranded DNA (ssDNA) act as a barrier to complete binding we measured whether these oligonucleotides are able to form stable secondary structures. We show that the preferential binding of recombination proteins is conserved among the three proteins and is influenced mainly by secondary structures in ssDNA.
authors.affiliation: Institut Curie, Section de Recherche UMR144-CNRS, 26 rue d'Ulm, F-75248-Paris Cedex 05, France.
authors.forename: E
authors.initials: E
authors.lastname: Biet
authors.forename: J
authors.initials: J
authors.lastname: Sun
authors.forename: M
authors.initials: M
authors.lastname: Dutreix
mesh_terms: D001483:Base Sequence; D017124:Conserved Sequence; D004277:DNA, Single-Stranded / Q000737:chemistry* / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D018900:Dinucleotide Repeats; D004926:Escherichia coli; D006358:Hot Temperature; D006801:Humans; D007700:Kinetics; D009690:Nucleic Acid Conformation; D009691:Nucleic Acid Denaturation; D011485:Protein Binding; D051135:Rad51 Recombinase; D011938:Rec A Recombinases / Q000378:metabolism; D011995:Recombination, Genetic; D012091:Repetitive Sequences, Nucleic Acid; D012441:Saccharomyces cerevisiae; D029701:Saccharomyces cerevisiae Proteins
chemical_list: D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins; D029701:Saccharomyces cerevisiae Proteins; C495151:RAD51 protein, S cerevisiae; C495153:RAD51 protein, human; D051135:Rad51 Recombinase; D011938:Rec A Recombinases