Biodesign

Korean Society for Structural Biology (한국구조생물학회)
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Crystal structure of unphosphorylated Spo0F from Paenisporosarcina sp. TG-14, a psychrophilic bacterium isolated from an Antarctic glacier

  • Lee, Chang Woo (Unit of Polar Genomics, Korea Polar Research Institute) ;
  • Park, Sun-Ha (Unit of Polar Genomics, Korea Polar Research Institute) ;
  • Jeong, Chang Sook (Unit of Polar Genomics, Korea Polar Research Institute) ;
  • Lee, Chang Sup (College of Pharmacy and Research Institute of Pharmaceutical Sciences, Gyeongsang National University) ;
  • Hong, Jong Wook (Department of Bionanotechnology, Graduate School, Hanyang University) ;
  • Park, Hyun Ho (College of Pharmacy, Chung-Ang University) ;
  • Park, Hyun (Unit of Polar Genomics, Korea Polar Research Institute) ;
  • Park, HaJeung (X-Ray Core, TRI, The Scripps Research Institute) ;
  • Lee, Jun Hyuck (Unit of Polar Genomics, Korea Polar Research Institute)
  • Received : 2018.11.01
  • Accepted : 2018.12.15
  • Published : 2018.12.31

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Abstract

Spo0F is a response regulator that modulates sporulation, undergoes phosphorylation for phosphorelay signal transduction, and interacts with various regulatory proteins; however, the mechanisms through which phosphorylation induces structural changes and regulates interactions with binding partners remain unclear. Here, we determined the unphosphorylated crystal structure of Spo0F from the psychrophilic bacterium Paenisporosarcina sp. TG-14 (PaSpo0F) and established a phosphorylation-state structural model. We found that PaSpo0F underwent structural changes (Lys54 and Lys102) by phosphorylation and generated new interactions (Lys102/Gln10 and Lys54/Glu84) to stabilize the ${\beta}4/{\alpha}4$ and ${\beta}1/{\alpha}1$ loop structures, which are important target-protein binding sites. Analysis of Bacillus subtilis Spo0 variants revealed movement by BsSpo0F Thr82 and Tyr84 residues following interaction with BsSpo0B, providing insight into the movement of corresponding residues in PaSpo0F (Thr80 and Tyr82), with further analysis of BsSpo0F/BsRapH interaction revealing alterations in the ${\beta}4/{\alpha}4$ loop region. These results suggest that phosphorylation-induced structural rearrangement might be essential for PaSpo0F activation and expand the understanding of Spo0F-specific activation mechanisms during sporulation.

Keywords

Acknowledgement

Supported by : Korea Polar Research Institute (KOPRI), National Research Foundation of Korea (NRF)

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