Nucleic Acids Research, Vol 24, Issue 11 2125-2132, Copyright © 1996 by Oxford University Press
SJ Sandler, LH Satin, HS Samra and AJ Clark
The process of homologous recombination has been documented in bacterial
and eucaryotic organisms. The Escherichia coli RecA and Saccharomyces
cerevisiae Rad51 proteins are the archetypal members of two related
families of proteins that play a central role in this process. Using the
PCR process primed by degenerate oligonucleotides designed to encode
regions of the proteins showing the greatest degree of identity, we
examined DNA from three organisms of a third phylogenetically divergent
group, Archaea, for sequences encoding proteins similar to RecA and Rad51.
The archaeans examined were a hyperthermophilic acidophile, Sulfolobus
sofataricus (Sso); a halophile, Haloferax volcanii (Hvo); and a
hyperthermophilic piezophilic methanogen, Methanococcus jannaschii (Mja).
The PCR generated DNA was used to clone a larger genomic DNA fragment
containing an open reading frame (orf), that we refer to as the radA gene,
for each of the three archaeans. As shown by amino acid sequence
alignments, percent amino acid identities and phylogenetic analysis, the
putative proteins encoded by all three are related to each other and to
both the RecA and Rad51 families of proteins. The putative RadA proteins
are more similar to the Rad51 family (approximately 40% identity at the
amino acid level) than to the RecA family (approximately 20%). Conserved
sequence motifs, putative tertiary structures and phylogenetic analysis
implied by the alignment are discussed. The 5' ends of mRNA transcripts to
the Sso radA were mapped. The levels of radA mRNA do not increase after
treatment with UV irradiation as do recA and RAD51 transcripts in E.coli
and S.cerevisiae. Hence it is likely that radA in this organism is a
constitutively expressed gene and we discuss possible implications of the
lack of UV-inducibility.
ARTICLES
recA-like genes from three archaean species with putative protein products similar to Rad51 and Dmc1 proteins of the yeast Saccharomyces cerevisiae
Department of Molecular and Cell Biology, Division of Genetics, University of California at Berkeley, Berkeley, CA 94720-3202, USA.
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