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- W2102118794 endingPage "1903" @default.
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- W2102118794 abstract "The RecA protein and other DNA strand exchange proteins are characterized by their ability to bind and pair DNA in a sequence-independent manner. In vitro selection experiments demonstrate, unexpectedly, that RecA protein has a preferential affinity for DNA sequences rich in GT composition. Such GT-rich sequences are present in loci that display increased recombinational activity in both eukaryotes and prokaryotes, including the Escherichia coli recombination hotspot, chi (5'-GCTGGTGG-3'). Interestingly, these selected sequences, or chi-containing substrates, display both an enhanced rate and extent of homologous pairing in RecA protein-dependent homologous pairing reactions. Thus, the binding and pairing of DNA by RecA protein is composition-dependent, suggesting that a component of the elevated recombinational activity of chi and increased genomic rearrangements at certain DNA sequences in eukaryotes is contributed by enhanced DNA pairing activity." @default.
- W2102118794 created "2016-06-24" @default.
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- W2102118794 date "1996-08-01" @default.
- W2102118794 modified "2023-09-26" @default.
- W2102118794 title "In vitro selection of preferred DNA pairing sequences by the Escherichia coli RecA protein." @default.
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- W2102118794 doi "https://doi.org/10.1101/gad.10.15.1890" @default.
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