Abstract
The SbcCD complex is an essential component of the DNA double-strand break (DSB) repair system in bacteria. The bacterial SbcCD complex recognizes and cleaves the DNA ends in DSBs by ATP-dependent endo- and exonuclease activities as an early step of the DNA repair process. SbcD consists of nuclease, cap**, and helix-loop-helix domains. Here, we present the crystal structure of a SbcD fragment from Staphylococcus aureus, which contained nuclease and cap** domains, at a resolution of 2.9 Å. This structure shows a dimeric assembly similar to that of the corresponding domains of SbcD from Escherichia coli. The S. aureus SbcD fragment exhibited endonuclease activities on supercoiled DNA and exonuclease activity on linear and nicked DNA. This study contributes to the understanding of the molecular basis for how bacteria can resist sterilizing treatment, causing DNA damage.
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Acknowledgements
This research was supported by the Bio & Medical Technology Development Program of the National Research Foundation (NRF) funded by the Ministry of Science & ICT (grant NRF-2017M3A9F6029755, NRF-2019M3E5D6063871). We made use of beamlines 11C at the Pohang Accelerator Laboratory (Pohang, Republic of Korea) and the MALS facility at the Korea Basic Science Institute (Ochang, Republic of Korea).
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Lee, J., Jo, I., Ahn, J. et al. Crystal structure of the nuclease and cap** domain of SbcD from Staphylococcus aureus. J Microbiol. 59, 584–589 (2021). https://doi.org/10.1007/s12275-021-1012-0
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DOI: https://doi.org/10.1007/s12275-021-1012-0