| Title | REVIEW] Recent paradigm shift in the assembly of bacterial tripartite efflux pumps and the type I secretion system |
|---|---|
| Author | Inseong Jo1, Jin-Sik Kim2, Yongbin Xu3, Jaekyung Hyun4, Kangseok Lee5, and Nam-Chul Ha1* |
| Address | 1Department of Agricultural Biotechnology, Center for Food Safety and Toxicology, Center for Food and Bioconvergence, Research Institute for Agriculture and Life Sciences, Seoul National University, Seoul 08826, Republic of Korea, 2Unit on Structural and Chemical Biology of Membrane Proteins, Cell Biology and Neurobiology Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA, 3Department of Bioengineering, College of Life Science, Dalian Minzu University, Dalian, 116600, Liaoning, P. R. China, 4Electron Microscopy Research Center, Korea Basic Science Institute, Cheongju 28119, Republic of Korea, 5Department of Life Science, Chung-Ang University, Seoul 06974, Republic of Korea |
| Bibliography | Journal of Microbiology, 57(3),185–194, 2019, |
| DOI | 10.1007/s12275-019-8520-1 |
| Key Words | multidrug resistance, multidrug efflux pump, structure, cryo-electron microscopy |
| Abstract | Tripartite efflux pumps and the type I secretion system of Gram-negative bacteria are large protein complexes that span the entire cell envelope. These complexes expel antibiotics and other toxic substances or transport protein toxins from bacterial cells. Elucidating the binary and ternary complex structures at an atomic resolution are crucial to understanding the assembly and working mechanism. Recent advances in cryoelectron microscopy along with the construction of chimeric proteins drastically shifted the assembly models. In this review, we describe the current assembly models from a historical perspective and emphasize the common assembly mechanism for the assembly of diverse tripartite pumps and type I secretion systems. |