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Haemolysin Coregulated Protein Is an Exported Receptor and Chaperone of Type VI Secretion Substrates
Open accessAbstract
SUMMARY Secretion systems require high fidelity mechanisms to discriminate substrates amongst the vast cytoplasmic pool of proteins. Factors mediating substrate recognition by the type VI secretion system (T6SS) of Gram-negative bacteria, a widespread pathway that translocates effector proteins into target bacterial cells, have not been defined. We report that haemolysin co-regulated protein (Hcp), a ring-shaped hexamer secreted by all characterized T6SSs, binds specifically to cognate effector molecules. Electron microscopy analysis of an Hcp–effector complex from Pseudomonas aeruginosa revealed the effector bound to the inner surface of Hcp. Further studies demonstrated that interaction with the Hcp pore is a general requirement for secretion of diverse effectors encompassing several enzymatic classes. Though previous models depict Hcp as a static conduit, our data indicate it is a chaperone and receptor of substrates. These unique functions of a secreted protein highlight fundamental differences between the export mechanism of T6 and other characterized secretory pathways.
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Type VII secretion — mycobacteria show the way
Abdallah, A. M., Gey van Pittius, N. C., DiGiuseppe Champion, P. A., Cox, J., Luirink, J., Vandenbroucke-Grauls, C. M. J. E., Appelmelk, B. J., & Bitter, W. (2007) · Nature Reviews Microbiology · doi:10.1038/nrmicro1773 · Cited by 763
Cited by
Secretion systems in Gram-negative bacteria: Structural and mechanistic insights
Costa, T. R. D., Felisberto-Rodrigues, C., Meir, A., Prevost, M. S., Redzej, A., Trokter, M., & Waksman, G. (2015) · Nature Reviews Microbiology · doi:10.1038/nrmicro3456 · Cited by 1,132
The Type VI secretion system: a versatile bacterial weapon
Coulthurst, S. (2019) · Microbiology · doi:10.1099/mic.0.000789 · Cited by 346
Structure of the T4 baseplate and its function in triggering sheath contraction
Taylor, N. M. I., Prokhorov, N. S., Guerrero-Ferreira, R. C., Shneider, M. M., Browning, C., Goldie, K. N., Stahlberg, H., & Leiman, P. G. (2016) · Nature · doi:10.1038/nature17971 · Cited by 299
Jiang, F., Waterfield, N. R., Yang, J., Yang, G., & Jin, Q. (2014) · Cell Host & Microbe · doi:10.1016/j.chom.2014.04.010 · Cited by 270
Whitney, J. C., Quentin, D., Sawai, S., LeRoux, M., Harding, B. N., Ledvina, H. E., Tran, B. Q., Robinson, H., Goo, Y. A., Goodlett, D. R., et al. (2015) · Cell · doi:10.1016/j.cell.2015.09.027 · Cited by 263
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Metadata
- Authors
- Silverman, J. M., Agnello, D. M., Zheng, H., Andrews, B. T., Li, M., Catalano, C. E., Gonen, T., & Mougous, J. D.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2013-09
- Volume
- 51
- Issue
- 5
- Pages
- 584-593
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2101820167
- Cited by
- 289
- References
- 1
- FWCI
- 15.38
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Silverman, J. M., Agnello, D. M., Zheng, H., Andrews, B. T., Li, M., Catalano, C. E., Gonen, T., & Mougous, J. D. (2013). Haemolysin Coregulated Protein Is an Exported Receptor and Chaperone of Type VI Secretion Substrates. Molecular Cell. https://doi.org/10.1016/j.molcel.2013.07.025
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