Literature DB >> 8622705

Rec-A protein-mediated irreversible fixation of an oligodeoxyribonucleotide to specific site in DNA.

E I Golub1, P M Glazer, D C Ward, C M Radding.   

Abstract

RecA protein can polymerize on an oligodeoxyribonucleotide to form a filament that finds its homologous sequence in double-stranded DNA. When such an oligonucleotide is linked to psoralen, a photoactivatable DNA intercalator, it irreversibly binds to the homologous site in double stranded DNA as a result of psoralen photoadduct formation at thymidines. The relative efficiency of specific vs. nonspecific binding of an oligonucleotide depended upon the ratio of psoralenated oligonucleotide to total DNA. Na+ ions at concentrations greater than 50 mM eliminated specific binding. Under optimal conditions. the probability of binding of an 80-mer oligonucleotide to a specific site was > 10(5) times greater than that of binding to any single nonspecific site. Under the conditions described, RecA-mediated photoadduction was equally efficient with superhelical and linear double-stranded DNA.

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Year:  1996        PMID: 8622705     DOI: 10.1016/0027-5107(95)00212-x

Source DB:  PubMed          Journal:  Mutat Res        ISSN: 0027-5107            Impact factor:   2.433


  1 in total

1.  Specific cleavage of DNA molecules at RecA-mediated triple-strand structure.

Authors:  Yasushi Shigemori; Michio Oishi
Journal:  Nucleic Acids Res       Date:  2004-01-02       Impact factor: 16.971

  1 in total

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