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Journal of Bacteriology, January 2000, p. 130-134, Vol. 182, No. 1
0021-9193/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Efficient Strand Transfer by the RadA Recombinase from the Hyperthermophilic Archaeon Desulfurococcus amylolyticus

Yuri V. Kil,1 Dmitry M. Baitin,1 Ryoji Masui,2 Elizaveta A. Bonch-Osmolovskaya,3 Seiki Kuramitsu,2 and Vladislav A. Lanzov1,*

Division of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute, Russian Academy of Sciences, Gatchina/St. Petersburg 188350,1 and Institute of Microbiology, Russian Academy of Sciences, Moskow 117811,3 Russia, and Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan2

Received 14 June 1999/Accepted 4 October 1999

The radA gene predicted to be responsible for homologous recombination in a hyperthermophilic archaeon, Desulfurococcus amylolyticus, was cloned, sequenced, and overexpressed in Escherichia coli cells. The deduced amino acid sequence of the gene product, RadA, was more similar to the human Rad51 protein (65% homology) than to the E. coli RecA protein (35%). A highly purified RadA protein was shown to exclusively catalyze single-stranded DNA-dependent ATP hydrolysis, which monitored presynaptic recombinational complex formation, at temperatures above 65°C (catalytic rate constant of 1.2 to 2.5 min-1 at 80 to 95°C). The RadA protein alone efficiently promoted the strand exchange reaction at the range of temperatures from 80 to 90°C, i.e., at temperatures approaching the melting point of DNA. It is noteworthy that both ATP hydrolysis and strand exchange are very efficient at temperatures optimal for host cell growth (90 to 92°C).

* Corresponding author. Mailing address: Petersburg Nuclear Physics Institute, RAS, Gatchina/St. Petersburg 188350, Russia. Phone and fax: 7 (812) 552 3019. E-mail: lanzov{at}lnpi.spb.su.

Journal of Bacteriology, January 2000, p. 130-134, Vol. 182, No. 1
0021-9193/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Haseltine, C. A., Kowalczykowski, S. C. (2009). An archaeal Rad54 protein remodels DNA and stimulates DNA strand exchange by RadA. Nucleic Acids Res 37: 2757-2770 [Abstract] [Full Text]  
  • Kil, Y. V., Glazunov, E. A., Lanzov, V. A. (2005). Characteristic Thermodependence of the RadA Recombinase from the Hyperthermophilic Archaeon Desulfurococcus amylolyticus. J. Bacteriol. 187: 2555-2557 [Abstract] [Full Text]  
  • Shalguev, V. I., Kil, Y. V., Yurchenko, L. V., Namsaraev, E. A., Lanzov, V. A. (2004). Rad51 Protein from the Thermotolerant Yeast Pichia angusta as a Typical but Thermodependent Member of the Rad51 Family. Eukaryot Cell 3: 1567-1573 [Abstract] [Full Text]  
  • Guy, C. P., Majernik, A. I., Chong, J. P. J., Bolt, E. L. (2004). A novel nuclease-ATPase (Nar71) from archaea is part of a proposed thermophilic DNA repair system. Nucleic Acids Res 32: 6176-6186 [Abstract] [Full Text]  
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