| Title | Crystal structure of the nuclease and capping domain of SbcD from Staphylococcus aureus |
|---|---|
| Author | Jinwook Lee1, Inseong Jo1, Jinsook Ahn1, Seokho Hong1, Soyeon Jeong1, Aeran Kwon2, and Nam-Chul Ha1* |
| Address | 1Research Institute of Agriculture and Life Sciences, Center for Food and Bioconvergence, Department of Agricultural Biotechnology, CALS, Seoul National University, Seoul 08826, Republic of Korea, 2Department of Beauty Care, College of Medical Science, Daegu Haany University, Gyeongsan 38610, Republic of Korea |
| Bibliography | Journal of Microbiology, 59(6),584–589, 2021, |
| DOI | 10.1007/s12275-021-1012-0 |
| Key Words | Staphylococcus aureus, SbcD, crystal structure, nuclease, DNA double strand breakage, DNA repair |
| 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, capping, and helix-loop-helix domains. Here, we present the crystal structure of a SbcD fragment from Staphylococcus aureus, which contained nuclease and capping 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. |