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Nucleic Acids Research Advance Access originally published online on March 12, 2009
Nucleic Acids Research 2009 37(8):2757-2770; doi:10.1093/nar/gkp068
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Nucleic Acids Research, 2009, Vol. 37, No. 8 2757-2770
© 2009 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Genome Integrity, Repair and Replication

An archaeal Rad54 protein remodels DNA and stimulates DNA strand exchange by RadA

Cynthia A. Haseltine1,2 and Stephen C. Kowalczykowski1,*

1Department of Microbiology and Department of Molecular and Cellular Biology, University of California, Davis, CA 95616-8665 and 2School of Molecular Biosciences, Washington State University, Pullman, WA 99163, USA

*To whom correspondence should be addressed. Tel: +1 530 752 5938; Fax: +1 530 752 5939; Email: sckowalczykowski{at}ucdavis.edu

Received November 2, 2008. Revised January 22, 2009. Accepted January 22, 2009.

Rad54 protein is a key member of the RAD52 epistasis group required for homologous recombination in eukaryotes. Rad54 is a duplex DNA translocase that remodels both DNA and protein–DNA complexes, and functions at multiple steps in the recombination process. Here we use biochemical criteria to demonstrate the existence of this important protein in a prokaryotic organism. The Sulfolobus solfataricus Rad54 (SsoRad54) protein is a double-strand DNA-dependent ATPase that can alter the topology of duplex DNA. Like its eukaryotic homolog, it interacts directly with the S. solfataricus Rad51 homologue, SsoRadA, to stimulate DNA strand exchange. Confirmation of this protein as an authentic Rad54 homolog establishes an essential phylogenetic bridge for identifying Rad54 homologs in the archaeal and bacterial domains.


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