@article {6414,
	title = {Haemolysin coregulated protein is an exported receptor and chaperone of type VI secretion substrates.},
	journal = {Molecular Cell},
	volume = {51},
	year = {2013},
	month = {2013 Sep 12},
	pages = {584-93},
	abstract = {<p>Secretion systems require high-fidelity mechanisms to discriminate substrates among 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 coregulated 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.</p>
},
	issn = {1097-4164},
	doi = {10.1016/j.molcel.2013.07.025},
	author = {Silverman, Julie M and Agnello, Danielle M and Zheng, Hongjin and Andrews, Benjamin T and Li, Mo and Catalano, Carlos E and Gonen, Tamir and Mougous, Joseph D}
}
