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Supramolecular Structure of the Salmonella typhimurium Type III Protein Secretion System

Kubori, Tomoko, Matsushima, Yukiyasu, Nakamura, Dai, Uralil, Jaimol, Lara-Tejero, Maria, Sukhan, Anand, Galán, Jorge E., Aizawa, Shin-Ichi·1998·Science

Abstract

The type III secretion system of Salmonella typhimurium directs the translocation of proteins into host cells. Evolutionarily related to the flagellar assembly machinery, this system is also present in other pathogenic bacteria, but its organization is unknown. Electron microscopy revealed supramolecular structures spanning the inner and outer membranes of flagellated and nonflagellated strains; such structures were not detected in strains carrying null mutations in components of the type III apparatus. Isolated structures were found to contain at least three proteins of this secretion system. Thus, the type III apparatus of S. typhimurium , and presumably other bacteria, exists as a supramolecular structure in the bacterial envelope.

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Metadata

Authors
Kubori, T., Matsushima, Y., Nakamura, D., Uralil, J., Lara-Tejero, M., Sukhan, A., Galán, J. E., & Aizawa, S.-I.
Venue
Science
Published
1998-04-24
Volume
280
Issue
5363
Pages
602-605
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2022873862
Cited by
896
References
0
FWCI
36.53
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Supramolecular Structure of the Salmonella typhimurium Type III Protein Secretion System. https://app.cochat.ai/papers/10.1126/science.280.5363.602
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Kubori, T., Matsushima, Y., Nakamura, D., Uralil, J., Lara-Tejero, M., Sukhan, A., Galán, J. E., & Aizawa, S.-I. (1998). Supramolecular Structure of the Salmonella typhimurium Type III Protein Secretion System. Science. https://doi.org/10.1126/science.280.5363.602

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.