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Chaperone release and unfolding of substrates in type III secretion

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  • Yukihiro Akeda

    (Yale University School of Medicine)

  • Jorge E. Galán

    (Yale University School of Medicine)

Abstract

Type III protein secretion systems are essential virulence factors of many bacteria pathogenic to humans, animals and plants1. These systems mediate the transfer of bacterial virulence proteins directly into the host cell cytoplasm. Proteins are thought to travel this pathway in a largely unfolded manner, and a family of customized cytoplasmic chaperones, which specifically bind cognate secreted proteins, are essential for secretion. Here we show that InvC, an ATPase associated with a Salmonella enterica type III secretion system2, has a critical function in substrate recognition. Furthermore, InvC induces chaperone release from and unfolding of the cognate secreted protein in an ATP-dependent manner. Our results show a similarity between the mechanisms of substrate recognition by type III protein secretion systems and AAA + ATPase disassembly machines.

Suggested Citation

  • Yukihiro Akeda & Jorge E. Galán, 2005. "Chaperone release and unfolding of substrates in type III secretion," Nature, Nature, vol. 437(7060), pages 911-915, October.
    • Handle: RePEc:nat:nature:v:437:y:2005:i:7060:d:10.1038_nature03992
    DOI: 10.1038/nature03992
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    Cited by:

    1. Xiaojiao Yang & Yanzhi Guo & Jiesi Luo & Xuemei Pu & Menglong Li, 2013. "Effective Identification of Gram-Negative Bacterial Type III Secreted Effectors Using Position-Specific Residue Conservation Profiles," PLOS ONE, Public Library of Science, vol. 8(12), pages 1-12, December.
    2. William R Taylor & Teige R S Matthews-Palmer & Morgan Beeby, 2016. "Molecular Models for the Core Components of the Flagellar Type-III Secretion Complex," PLOS ONE, Public Library of Science, vol. 11(11), pages 1-33, November.
    3. Manuel Halte & Ekaterina P. Andrianova & Christian Goosmann & Fabienne F. V. Chevance & Kelly T. Hughes & Igor B. Zhulin & Marc Erhardt, 2024. "FlhE functions as a chaperone to prevent formation of periplasmic flagella in Gram-negative bacteria," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    4. Dominic Gilzer & Madeleine Schreiner & Hartmut H. Niemann, 2022. "Direct interaction of a chaperone-bound type III secretion substrate with the export gate," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    5. Vidhyavathi Raman & Clemencia M. Rojas & Balaji Vasudevan & Kevin Dunning & Jaydeep Kolape & Sunhee Oh & Jianfei Yun & Lishan Yang & Guangming Li & Bikram D. Pant & Qingzhen Jiang & Kirankumar S. Myso, 2022. "Agrobacterium expressing a type III secretion system delivers Pseudomonas effectors into plant cells to enhance transformation," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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