The DNA binding and pairing preferences of the archaeal RadA protein demonstrate a universal characteristic of DNA strand exchange proteins.
The archaeal RadA protein is a homologue of the Escherichia coli RecA and Saccharomyces cerevisiae Rad51 proteins and possesses the same biochemical activities. Here, using in vitro selection, we show that the Sulfolobus solfataricus RadA protein displays the same preference as its homologues for binding to DNA sequences that are rich in G residues, and under-represented in A and C residues. The RadA protein also displays enhanced pairing activity with these in vitro-selected sequences. These parallels between the archaeal, eukaryal and bacterial proteins further extend the universal characteristics of DNA strand exchange proteins.
Division of Biological Sciences, Sections of Microbiology and of Molecular and Cellular Biology, Microbiology Graduate Group, Hutchison Hall, Room 258, University of California, Davis, CA 95616-8665, USA.
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Seitz
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Kowalczykowski
D019843:Archaeal Proteins / Q000235:genetics / Q000378:metabolism*; D019641:DNA, Archaeal / Q000235:genetics / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins; D011485:Protein Binding; D016944:Sulfolobus / Q000235:genetics / Q000378:metabolism*
D019843:Archaeal Proteins; D019641:DNA, Archaeal; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C491059:RadA protein, E coli; C117252:RadA protein, archaeal