Chaperone release and unfolding of substrates in type III secretion
Type III protein secretion systems are essential virulence factors of many bacteria pathogenic to humans, animals and plants. 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 ma...
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| Published in: | Nature Vol. 437; no. 7060; pp. 911 - 915 |
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| Main Authors: | , |
| Format: | Journal Article |
| Language: | English |
| Published: |
London
Nature Publishing
06-10-2005
Nature Publishing Group |
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| Abstract | Type III protein secretion systems are essential virulence factors of many bacteria pathogenic to humans, animals and plants. 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 system, 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. |
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| AbstractList | Type III protein secretion systems are essential virulence factors of many bacteria pathogenic to humans, animals and plants. 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 system, 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. 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. [PUBLICATION ABSTRACT] |
| Audience | Academic |
| Author | Akeda, Yukihiro Galán, Jorge E |
| Author_xml | – givenname: Jorge E surname: Galán fullname: Galán, Jorge E – givenname: Yukihiro surname: Akeda fullname: Akeda, Yukihiro |
| BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17156945$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/16208377$$D View this record in MEDLINE/PubMed |
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| CODEN | NATUAS |
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| ContentType | Journal Article |
| Copyright | 2006 INIST-CNRS COPYRIGHT 2005 Nature Publishing Group Copyright Nature Publishing Group Oct 6, 2005 |
| Copyright_xml | – notice: 2006 INIST-CNRS – notice: COPYRIGHT 2005 Nature Publishing Group – notice: Copyright Nature Publishing Group Oct 6, 2005 |
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| Keywords | Salmonella Bacteria Type III secretion system Chaperone Enterobacteriaceae |
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| SubjectTerms | Bacterial Proteins - chemistry Bacterial Proteins - metabolism Bacterial Proteins - secretion Bacteriology Biological and medical sciences Cells Chaperonin 60 - chemistry Chaperonin 60 - metabolism Fundamental and applied biological sciences. Psychology Microbiology Molecular Chaperones - chemistry Molecular Chaperones - metabolism Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains Pathogens Protein Folding Protein Tyrosine Phosphatases - chemistry Protein Tyrosine Phosphatases - metabolism Proteins Proton-Translocating ATPases - metabolism Salmonella enterica - chemistry Salmonella enterica - enzymology Salmonella enterica - metabolism Salmonella enterica - pathogenicity Substrate Specificity Substrates Virulence Factors - chemistry Virulence Factors - metabolism |
| Title | Chaperone release and unfolding of substrates in type III secretion |
| URI | http://dx.doi.org/10.1038/nature03992 https://www.ncbi.nlm.nih.gov/pubmed/16208377 https://www.proquest.com/docview/204570284 https://search.proquest.com/docview/17645293 https://search.proquest.com/docview/27994840 https://search.proquest.com/docview/68664102 |
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