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

1998/05/01 by Erica M. Seitz, E. M. Seitz, Joel Brockman +7 · 2 citations
Biochemistry, Genetics and Molecular Biology · #Bacterial Genetics and Biotechnology #Cancer therapeutics and mechanisms #DNA Repair Mechanisms

paper · pdf · doi:10.1101/gad.12.9.1248

openalex publication_date 1998/05/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/30

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.

Cited by

• Eukaryotic Recombinases Duplicated After Divergence From Known Asgard Archaeal RadA: Implications for the Evolution of Sex During Eukaryogenesis
• Sexual Communication in Archaea, the Precursor to Eukaryotic Meiosis

Related

• Extraction of Deep Phylogenetic Signal and Improved Resolution of Evolutionary Events within the recA/RAD51 Phylogeny
• Many nonuniversal archaeal ribosomal proteins are found in conserved gene clusters
• Structural mechanism of strand exchange by the RAD51 filament
• Archaeal DNA Replication
• Eukaryotic Recombinases Duplicated After Divergence From Known Asgard Archaeal RadA: Implications for the Evolution of Sex During Eukaryogenesis