Characterization of an archaeal recombinase paralog that exhibits novel anti-recombinase activity.

Corey Knadler, Michael Rolfsmeier, Antonia Vallejo, Cynthia Haseltine

Mutation research 2020 May - Dec

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The process of homologous recombination is heavily dependent on the RecA family of recombinases for repair of DNA double-strand breaks. These recombinases are responsible for identifying homologies and forming heteroduplex DNA between substrate ssDNA and dsDNA templates, activities that are modified by various accessory factors. In this work we describe the biochemical functions of the SsoRal2 recombinase paralog from the crenarchaeon Sulfolobus solfataricus. We found that the SsoRal2 protein is a DNA-independent ATPase that, unlike the other S. solfataricus paralogs, does not bind either ss- or dsDNA. Instead, SsoRal2 alters the ssDNA binding activity of the SsoRadA recombinase in conjunction with another paralog, SsoRal1. In the presence of SsoRal1, SsoRal2 has a modest effect on strand invasion but effectively abrogates strand exchange activity. Taken together, these results indicate that SsoRal2 assists in nucleoprotein filament modulation and control of strand exchange in S. solfataricus. Copyright © 2020 Elsevier B.V. All rights reserved.

Citation

Corey Knadler, Michael Rolfsmeier, Antonia Vallejo, Cynthia Haseltine. Characterization of an archaeal recombinase paralog that exhibits novel anti-recombinase activity. Mutation research. 2020 May - Dec;821:111703