RadA protein is an archaeal RecA protein homolog that catalyzes DNA strand exchange
AUTOR(ES)
Seitz, Erica M.
FONTE
Cold Spring Harbor Laboratory Press
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=316774Documentos Relacionados
- recA protein promotes homologous-pairing and strand-exchange reactions between duplex DNA molecules.
- A novel pairing process promoted by Escherichia coli RecA protein: inverse DNA and RNA strand exchange
- recA protein of Escherichia coli promotes branch migration, a kinetically distinct phase of DNA strand exchange.
- Torsional stress generated by RecA protein during DNA strand exchange separates strands of a heterologous insert.
- Torsional stress generated by RecA protein during DNA strand exchange separates strands of a heterologous insert