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

Erica M. Seitz, Joel P. Brockman, Steven J. Sandler, A. John Clark, Stephen C. Kowalczykowski

Research output: Contribution to journalArticle

134 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1248-1253
Number of pages6
JournalGenes and Development
Volume12
Issue number9
StatePublished - May 1 1998

Keywords

  • Archaea
  • DNA strand exchange
  • RadA
  • RecA
  • Recombination

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

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    Seitz, E. M., Brockman, J. P., Sandler, S. J., Clark, A. J., & Kowalczykowski, S. C. (1998). RadA protein is an archaeal RecA protein homolog that catalyzes DNA strand exchange. Genes and Development, 12(9), 1248-1253.