TY - JOUR
T1 - Assembly of the inner rod determines needle length in the type III secretion injectisome
AU - Marlovits, Thomas C.
AU - Kubori, Tomoko
AU - Lara-Tejero, María
AU - Thomas, Dennis
AU - Unger, Vinzenz M.
AU - Galán, Jorge E.
N1 - Funding Information:
Acknowledgements We thank members of the Galán laboratory for critical reviews of this manuscript. We are also grateful to the Yale School of Medicine for the support of the Cryo Electron Microscopy Core Facility. Molecular graphic images were produced using the Chimera package from the Computer Graphics Laboratory, University of California, San Francisco (supported by the NIH). This work was supported by grants from the National Institutes of Health (to V.M.U. and J.E.G.).
PY - 2006/6/1
Y1 - 2006/6/1
N2 - Assembly of multi-component supramolecular machines is fundamental to biology, yet in most cases, assembly pathways and their control are poorly understood. An example is the type III secretion machine, which mediates the transfer of bacterial virulence proteins into host cells. A central component of this nanomachine is the needle complex or injectisome, an organelle associated with the bacterial envelope that is composed of a multi-ring base, an inner rod, and a protruding needle. Assembly of this organelle proceeds in sequential steps that require the reprogramming of the secretion machine. Here we provide evidence that, in Salmonella typhimurium, completion of the assembly of the inner rod determines the size of the needle substructure. Assembly of the inner rod, which is regulated by the InvJ protein, triggers conformational changes on the cytoplasmic side of the injectisome, reprogramming the secretion apparatus to stop secretion of the needle protein.
AB - Assembly of multi-component supramolecular machines is fundamental to biology, yet in most cases, assembly pathways and their control are poorly understood. An example is the type III secretion machine, which mediates the transfer of bacterial virulence proteins into host cells. A central component of this nanomachine is the needle complex or injectisome, an organelle associated with the bacterial envelope that is composed of a multi-ring base, an inner rod, and a protruding needle. Assembly of this organelle proceeds in sequential steps that require the reprogramming of the secretion machine. Here we provide evidence that, in Salmonella typhimurium, completion of the assembly of the inner rod determines the size of the needle substructure. Assembly of the inner rod, which is regulated by the InvJ protein, triggers conformational changes on the cytoplasmic side of the injectisome, reprogramming the secretion apparatus to stop secretion of the needle protein.
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U2 - 10.1038/nature04822
DO - 10.1038/nature04822
M3 - Article
C2 - 16738660
AN - SCOPUS:33745279057
SN - 0028-0836
VL - 441
SP - 637
EP - 640
JO - Nature
JF - Nature
IS - 7093
ER -