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

نویسندگان

  • E M Seitz
  • J P Brockman
  • S J Sandler
  • A J Clark
  • S C Kowalczykowski
چکیده

With the discovery that the Saccharomyces cerevisiae Rad51 protein is both structurally and functionally similar to the Escherichia 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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The DNA binding and pairing preferences of the archaeal RadA protein demonstrate a universal characteristic of DNA strand exchange proteins.

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عنوان ژورنال:
  • Genes & development

دوره 12 9  شماره 

صفحات  -

تاریخ انتشار 1998