RadA protein is an archaeal RecA protein homolog that catalyzes DNA strand exchange

  1. Erica M. Seitz,
  2. Joel P. Brockman,
  3. Steven J. Sandler,
  4. A. John Clark, and
  5. Stephen C. Kowalczykowski
  1. Division of Biological Sciences, Sections of Microbiology and Molecular and Cellular Biology, Microbiology Graduate Group, and Biochemistry and Molecular Biology Graduate Group, University of California, Davis, California 95616-8665 USA; Department of Molecular and Cell Biology, Division of Genetics, University of California at Berkeley, Berkeley, California 94702-3202 USA

Abstract

With the discovery that the Saccharomyces cerevisiaeRad51 protein is both structurally and functionally similar to theEscherichia coli RecA protein, the RecA paradigm for homologous recombination was extended to the Eucarya. The ubiquitous presence of RecA and Rad51 protein homologs raises the question of whether this archetypal protein exists within the third domain of life, the Archaea. Here we present the isolation of a Rad51/RecA protein homolog from the archaeon Sulfolobus solfataricus, and show that this protein, RadA, possesses the characteristics of a DNA strand exchange protein: The RadA protein is a DNA-dependent ATPase, forms a nucleoprotein filament on DNA, and catalyzes DNA pairing and strand exchange.

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Footnotes

  • Corresponding author.

  • E-MAIL sckowalczykowski{at}ucdavis.edu; FAX (530) 752-5939.

    • Received December 29, 1997.
    • Accepted March 2, 1998.
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