Abstract
Archaea have recombination proteins similar to those of eukaryote, but many have not been characterized. Here, the characterization of a Rad55 homologue from Sulfolobus tokodaii (stRad55A) was reported. StRad55A protein preferred binding to ssDNA and had ssDNA-dependent ATPase activity. In addition, UV light could induce the expression of this protein, which was different from RadB, a RadA paralog found in euryarchaeota. Most importantly, stRad55A could release the suppression of excessive stSSB (single strand DNA binding protein from S. tokodaii) on the strand exchange catalyzed by stRadA (RadA homologue from S. tokodaii), by interacting directly with both stRadA and stSSB. StRad55A may function as a mediator to accelerate the displacement of stSSB by stRadA.
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Acknowledgments
This work was supported by the National Basic Research Program of China (2004CB719604) and National Natural Science Foundation of China (30470386 and 30700011).
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Communicated by J.N. Reeve.
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Appendix Figure Phylogenetic analysis based on the entire amino acid sequences of the Rad51/RadA and their paralogs from Arabidopsis thaliana, Halobacterium salinarum, Homo sapiens, Methanococcus jannaschii, Natronomonas pharaonis, Pyrococcus furiosus, Saccharomyces cerevisiae, Sulfolobus solfataricus, and Sulfolobus tokodaii. The sequences were obtained from GenBank and followed by a multiple sequence alignment by ClustalX. The phylogenetic tree was inferred from the alignment information using parsimony method. (DOC 122 kb)
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Sheng, D., Zhu, S., Wei, T. et al. The in vitro activity of a Rad55 homologue from Sulfolobus tokodaii, a candidate mediator in RadA-catalyzed homologous recombination. Extremophiles 12, 147–157 (2008). https://doi.org/10.1007/s00792-007-0113-y
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DOI: https://doi.org/10.1007/s00792-007-0113-y