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In vitro selection of preferred DNA pairing sequences by the Escherichia coli RecA protein.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Tracy, R. B. Kowalczykowski, Stephen C. |
| Copyright Year | 1996 |
| 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. |
| File Format | PDF HTM / HTML |
| DOI | 10.1101/gad.10.15.1890 |
| Alternate Webpage(s) | http://genesdev.cshlp.org/content/10/15/1890.full.pdf |
| PubMed reference number | 8756347 |
| Alternate Webpage(s) | https://doi.org/10.1101/gad.10.15.1890 |
| Journal | Medline |
| Volume Number | 10 |
| Issue Number | 15 |
| Journal | Genes & development |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
