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Originally published In Press as doi:10.1074/jbc.M004556200 on July 7, 2000

J. Biol. Chem., Vol. 275, Issue 43, 33791-33797, October 27, 2000
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Domain Analysis of an Archaeal RadA Protein for the Strand Exchange Activity*

Kayoko KomoriDagger , Tomoko Miyata§, Hiromi Daiyasu, Hiroyuki Toh, Hideo Shinagawa||, and and, Yoshizumi IshinoDagger **

From the Departments of Dagger  Molecular Biology, § Structural Biology, and  Bioinformatics, Biomolecular Engineering Research Institute, Suita, Osaka 565-0874, Japan and the || Department of Molecular Microbiology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, Japan

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 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 divided 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.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

** To whom correspondence should be addressed: Dept. of Molecular Biology, Biomolecular Engineering Research Inst., 6-2-3 Furuedai, Suita, Osaka 565-0874, Japan. Tel.: 81-6-6872-8208; Fax: 81-6-6872-8219; E-mail: ishino@beri.co.jp.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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