Molecules and Cells

Korean Society for Molecular and Cellular Biology (한국분자세포생물학회)
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Structure and Function of the Autolysin SagA in the Type IV Secretion System of Brucella abortus

  • Hyun, Yongseong (Department of Agricultural Biotechnology, Research Institute for Agriculture and Life Sciences, Center for Food and Bioconvergence, CALS, Seoul National University) ;
  • Baek, Yeongjin (Department of Agricultural Biotechnology, Research Institute for Agriculture and Life Sciences, Center for Food and Bioconvergence, CALS, Seoul National University) ;
  • Lee, Chanyoung (Department of Agricultural Biotechnology, Research Institute for Agriculture and Life Sciences, Center for Food and Bioconvergence, CALS, Seoul National University) ;
  • Ki, Nayeon (Department of Agricultural Biotechnology, Research Institute for Agriculture and Life Sciences, Center for Food and Bioconvergence, CALS, Seoul National University) ;
  • Ahn, Jinsook (Department of Agricultural Biotechnology, Research Institute for Agriculture and Life Sciences, Center for Food and Bioconvergence, CALS, Seoul National University) ;
  • Ryu, Sangryeol (Department of Agricultural Biotechnology, Research Institute for Agriculture and Life Sciences, Center for Food and Bioconvergence, CALS, Seoul National University) ;
  • Ha, Nam-Chul (Department of Agricultural Biotechnology, Research Institute for Agriculture and Life Sciences, Center for Food and Bioconvergence, CALS, Seoul National University)
  • Received : 2021.01.15
  • Accepted : 2021.02.17
  • Published : 2021.07.31
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Abstract

A recent genetic study with Brucella abortus revealed the secretion activator gene A (SagA) as an autolysin component creating pores in the peptidoglycan (PGN) layer for the type IV secretion system (T4SS) and peptidoglycan hydrolase inhibitor A (PhiA) as an inhibitor of SagA. In this study, we determined the crystal structures of both SagA and PhiA. Notably, the SagA structure contained a PGN fragment in a space between the N- and C-terminal domains, showing the substrate-dependent hinge motion of the domains. The purified SagA fully hydrolyzed the meso-diaminopimelic acid (DAP)-type PGN, showing a higher activity than hen egg-white lysozyme. The PhiA protein exhibiting tetrameric assembly failed to inhibit SagA activity in our experiments. Our findings provide implications for the molecular basis of the SagA-PhiA system of B. abortus. The development of inhibitors of SagA would further contribute to controlling brucellosis by attenuating the function of T4SS, the major virulence factor of Brucella.

Keywords

Acknowledgement

This research was supported by Agriculture, Food, and Rural Affairs Convergence Technologies Program for Educating Creative Global Leader (710012-03-1-HD120). This research was also supported by the Bio & Medical Technology Development Program of the National Research Foundation (NRF) funded by the Korean government (MSIT) (NRF-2017M3A9F6029755). We made use of beamlines 5C and 11C at the Pohang Accelerator Laboratory (Pohang, Republic of Korea). This work was also supported by the BK21 Plus Program of the Department of Agricultural Biotechnology, Seoul National University, Seoul, Korea.

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