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

TitleRadA protein is an archaeal RecA protein homolog that catalyzes DNA strand exchange.
Publication TypeJournal Article
Year of Publication1998
AuthorsSeitz EM, Brockman JP, Sandler SJ, Clark AJ, Kowalczykowski SC
JournalGenes Dev
Volume12
Issue9
Pagination1248-53
Date Published1998 May 1
ISSN0890-9369
KeywordsAdenosine Triphosphatases, Archaeal Proteins, Bacterial Proteins, DNA Helicases, DNA, Archaeal, DNA-Binding Proteins, Escherichia coli, Escherichia coli Proteins, Genes, Archaeal, Nucleoproteins, Rad51 Recombinase, Rec A Recombinases, Recombinant Proteins, Recombination, Genetic, Sulfolobus
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.

Alternate JournalGenes Dev.
PubMed ID9573041