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- W3022139318 abstract "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." @default.
- W3022139318 created "2020-05-13" @default.
- W3022139318 creator A5008060522 @default.
- W3022139318 creator A5057190203 @default.
- W3022139318 creator A5069960736 @default.
- W3022139318 creator A5081949268 @default.
- W3022139318 date "2020-05-01" @default.
- W3022139318 modified "2023-10-01" @default.
- W3022139318 title "Characterization of an archaeal recombinase paralog that exhibits novel anti-recombinase activity" @default.
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- W3022139318 doi "https://doi.org/10.1016/j.mrfmmm.2020.111703" @default.
- W3022139318 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/32416400" @default.
- W3022139318 hasPublicationYear "2020" @default.
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