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Journal of Bacteriology, April 2005, p. 2555-2557, Vol. 187, No. 7
0021-9193/05/$08.00+0     doi:10.1128/JB.187.7.2555-2557.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Characteristic Thermodependence of the RadA Recombinase from the Hyperthermophilic Archaeon Desulfurococcus amylolyticus

Yury V. Kil, Eugene A. Glazunov, and Vladislav A. Lanzov*

Division of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute, Russian Academy of Sciences, Gatchina/St. Petersburg, Russia

Received 5 November 2004/ Accepted 29 December 2004

The Desulfurococcus amylolyticus RadA protein (RadADa) promotes recombination at temperatures approaching the DNA melting point. Here, analyzing ATPase of the RadADa presynaptic complex, we described other distinguishing characteristics of RadADa. These include sensitivity to NaCl, preference for lengthy single-stranded DNA as a cofactor, protein activity at temperatures of over 100°C, and bimodal ATPase activity. These characteristics suggest that RadADa is a founding member of a new class of archaeal recombinases.

* Corresponding author. Mailing address: Division of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute, Russian Academy of Sciences, Gatchina/St. Petersburg 188300, Russia. Phone: 7-812-2473141. Fax: 7-812-2473141. E-mail: vlanzov{at}bpc.spbstu.ru.

Journal of Bacteriology, April 2005, p. 2555-2557, Vol. 187, No. 7
0021-9193/05/$08.00+0     doi:10.1128/JB.187.7.2555-2557.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.





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