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, χ (5'-GCTGGTGG-3'). Interestingly, these selected sequences, or χ-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 χ and increased genomic rearrangements at certain DNA sequences in eukaryotes is contributed by enhanced DNA pairing activity.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1890-1903 |
| Number of pages | 14 |
| Journal | Genes and Development |
| Volume | 10 |
| Issue number | 15 |
| State | Published - 1996 |
Keywords
- χ
- GT-rich sequences
- Homologous recombination
- in vitro selection
- RecA protein
ASJC Scopus subject areas
- Genetics
- Developmental Biology