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Papers In Press, published online ahead of print July 7, 2000
Department of Molecular Biology, Biomolecular Engineering Resaerch Institute, Suita, Osaka 565-0874
Corresponding Author: ishino{at}beri.co.jp
Archaeal RadA, like eukaryotic Rad51 and bacterial RecA, promotes strand exchange between DNA strands with homologous sequences in vitro, and is believed to participate in the homologous recombination in cells. The amino acid sequences of the archaeal RadA proteins are more similar to the eukaryotic Rad51s rather than the bacterial RecAs, and especially, the N-terminal region containing Domain I is conserved among the RadA and Rad51 proteins, but is absent from RecA. To understand the structure-function relationship of RadA, we devided the RadA protein from Pyrococcus furiosus into two parts, the N-terminal one-third (RadA-n) and the residual C-terminal two-thirds (RadA-c), the latter of which contains the central core domain (Domain II) of the RecA/Rad51 family proteins. RadA-c had the DNA-dependent ATPase activity and the strand exchange activity by itself, although much weaker (10 %) than that of the intact RadA. These activities of RadA-c were restored to 60 % of those of RadA by addition of RadA-n, indicating that the proper active structure of RadA was reconstituted in vitro. These results suggest that the basic activities of the RecA/Rad51 family proteins for homologous recombination are derived from Domain II, and the N-terminal region may help to enhance the catalytic efficiencies.
J. Biol. Chem, 10.1074/jbc.M004556200
Submitted on May 26, 2000
Revised on June 30, 2000
Accepted on July 6, 2000
Domain analysis of an archaeal RadA protein for the strand exchange activity
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