Organization and coordinated assembly of the type III secretion export apparatus.
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Organization and coordinated assembly of the type III secretion export apparatus. / Wagner, Samuel; Königsmaier, Lisa; Lara-Tejero, María; Lefebre, Matthew; Marlovits, Thomas; Galán, Jorge E.
In: P NATL ACAD SCI USA, Vol. 107, No. 41, 41, 2010, p. 17745-17750.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - Organization and coordinated assembly of the type III secretion export apparatus.
AU - Wagner, Samuel
AU - Königsmaier, Lisa
AU - Lara-Tejero, María
AU - Lefebre, Matthew
AU - Marlovits, Thomas
AU - Galán, Jorge E
PY - 2010
Y1 - 2010
N2 - Type III protein secretion systems are unique bacterial nanomachines with the capacity to deliver bacterial effector proteins into eukaryotic cells. These systems are critical to the biology of many pathogenic or symbiotic bacteria for insects, plants, animals, and humans. Essential components of these systems are multiprotein envelope-associated organelles known as the needle complex and a group of membrane proteins that compose the so-called export apparatus. Here, we show that components of the export apparatus associate intimately with the needle complex, forming a structure that can be visualized by cryo-electron microscopy. We also show that formation of the needle complex base is initiated at the export apparatus and that, in the absence of export apparatus components, there is a significant reduction in the levels of needle complex base assembly. Our results show a substantial coordination in the assembly of the two central elements of type III secretion machines.
AB - Type III protein secretion systems are unique bacterial nanomachines with the capacity to deliver bacterial effector proteins into eukaryotic cells. These systems are critical to the biology of many pathogenic or symbiotic bacteria for insects, plants, animals, and humans. Essential components of these systems are multiprotein envelope-associated organelles known as the needle complex and a group of membrane proteins that compose the so-called export apparatus. Here, we show that components of the export apparatus associate intimately with the needle complex, forming a structure that can be visualized by cryo-electron microscopy. We also show that formation of the needle complex base is initiated at the export apparatus and that, in the absence of export apparatus components, there is a significant reduction in the levels of needle complex base assembly. Our results show a substantial coordination in the assembly of the two central elements of type III secretion machines.
KW - Image Processing, Computer-Assisted
KW - Blotting, Western
KW - Immunoprecipitation
KW - Cryoelectron Microscopy
KW - Bacterial Proteins/metabolism
KW - Membrane Transport Proteins/metabolism
KW - Multiprotein Complexes/metabolism/ultrastructure
KW - Salmonella typhimurium/metabolism/physiology/ultrastructure
KW - Secretory Pathway/physiology
KW - Image Processing, Computer-Assisted
KW - Blotting, Western
KW - Immunoprecipitation
KW - Cryoelectron Microscopy
KW - Bacterial Proteins/metabolism
KW - Membrane Transport Proteins/metabolism
KW - Multiprotein Complexes/metabolism/ultrastructure
KW - Salmonella typhimurium/metabolism/physiology/ultrastructure
KW - Secretory Pathway/physiology
M3 - SCORING: Journal article
VL - 107
SP - 17745
EP - 17750
JO - P NATL ACAD SCI USA
JF - P NATL ACAD SCI USA
SN - 0027-8424
IS - 41
M1 - 41
ER -
