Structure of a pathogenic type 3 secretion system in action
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Structure of a pathogenic type 3 secretion system in action. / Radics, Julia; Königsmaier, Lisa; Marlovits, Thomas C.
in: NAT STRUCT MOL BIOL, Jahrgang 21, Nr. 1, 01.01.2014, S. 82-7.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Structure of a pathogenic type 3 secretion system in action
AU - Radics, Julia
AU - Königsmaier, Lisa
AU - Marlovits, Thomas C
PY - 2014/1/1
Y1 - 2014/1/1
N2 - Type 3 secretion systems use 3.5-megadalton syringe-like, membrane-embedded 'injectisomes', each containing an ~800-Å-long needle complex to connect intracellular compartments of infectious bacteria and hosts. Here we identify requirements for substrate association with, transport through and exit from the injectisome of Salmonella enterica serovar Typhimurium. This guided the design of substrates that become trapped within the secretion path and enabled visualization of injectisomes in action in situ. We used cryo-EM to define the secretion path, providing a structural explanation as to why effector proteins must be unfolded during transport. Furthermore, trapping of a heterologous substrate in the needle prevents secretion of natural bacterial effectors. Together, the data reveal the path of protein secretion across multiple membranes and show that mechanisms rejecting unacceptable substrates can be undermined, and transport of bacterial effectors across an already assembled type 3 secretion system can be inhibited.
AB - Type 3 secretion systems use 3.5-megadalton syringe-like, membrane-embedded 'injectisomes', each containing an ~800-Å-long needle complex to connect intracellular compartments of infectious bacteria and hosts. Here we identify requirements for substrate association with, transport through and exit from the injectisome of Salmonella enterica serovar Typhimurium. This guided the design of substrates that become trapped within the secretion path and enabled visualization of injectisomes in action in situ. We used cryo-EM to define the secretion path, providing a structural explanation as to why effector proteins must be unfolded during transport. Furthermore, trapping of a heterologous substrate in the needle prevents secretion of natural bacterial effectors. Together, the data reveal the path of protein secretion across multiple membranes and show that mechanisms rejecting unacceptable substrates can be undermined, and transport of bacterial effectors across an already assembled type 3 secretion system can be inhibited.
KW - Bacterial Proteins
KW - Protein Conformation
KW - Protein Transport
KW - Salmonella enterica
U2 - 10.1038/nsmb.2722
DO - 10.1038/nsmb.2722
M3 - SCORING: Journal article
C2 - 24317488
VL - 21
SP - 82
EP - 87
JO - NAT STRUCT MOL BIOL
JF - NAT STRUCT MOL BIOL
SN - 1545-9993
IS - 1
ER -