Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system
Abstract
The flagellum and the injectisome enable bacterial locomotion and pathogenesis, respectively. These nanomachines assemble and function using a type III secretion system (T3SS). Exported proteins are delivered to the export apparatus by dedicated cytoplasmic chaperones for their transport through the membrane. The structural and mechanistic basis of this process is poorly understood. Here we report the structures of two ternary complexes among flagellar chaperones (FliT and FliS), protein substrates (the filament-capping FliD and flagellin FliC), and the export gate platform protein FlhA. The substrates do not interact directly with FlhA; however, they are required to induce a binding-competent conformation to the chaperone that exposes the recognition motif featuring a highly conserved sequence recognized by FlhA. The structural data reveal the recognition signal in a class of T3SS proteins and provide new insight into the assembly of key protein complexes at the export gate.
- Authors:
-
[1];
[1]
- St. Jude Children’s Research Hospital, Memphis, TN (United States)
- Univ. of Minnesota, Minneapolis, MN (United States)
- Katholicke Univ. Leuven (Belgium)
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES). Scientific User Facilities Division; US National Inst. of Health; NIH-ORIP HEI
- OSTI Identifier:
- 1436776
- Grant/Contract Number:
- AC02-06CH11357; AI094623; NIGMS P41-GM103403; S10 RR029205
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Nature Communications
- Additional Journal Information:
- Journal Volume: 9; Journal Issue: 1; Journal ID: ISSN 2041-1723
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; Bacterial secretion; Bacterial structural biology; NMR spectroscopy; X-ray crystallography
Citation Formats
Xing, Qiong, Shi, Ke, Portaliou, Athina, Rossi, Paolo, Economou, Anastassios, and Kalodimos, Charalampos G. Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system. United States: N. p., 2018.
Web. doi:10.1038/s41467-018-04137-4.
Xing, Qiong, Shi, Ke, Portaliou, Athina, Rossi, Paolo, Economou, Anastassios, & Kalodimos, Charalampos G. Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system. United States. https://doi.org/10.1038/s41467-018-04137-4
Xing, Qiong, Shi, Ke, Portaliou, Athina, Rossi, Paolo, Economou, Anastassios, and Kalodimos, Charalampos G. Wed .
"Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system". United States. https://doi.org/10.1038/s41467-018-04137-4. https://www.osti.gov/servlets/purl/1436776.
@article{osti_1436776,
title = {Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system},
author = {Xing, Qiong and Shi, Ke and Portaliou, Athina and Rossi, Paolo and Economou, Anastassios and Kalodimos, Charalampos G.},
abstractNote = {The flagellum and the injectisome enable bacterial locomotion and pathogenesis, respectively. These nanomachines assemble and function using a type III secretion system (T3SS). Exported proteins are delivered to the export apparatus by dedicated cytoplasmic chaperones for their transport through the membrane. The structural and mechanistic basis of this process is poorly understood. Here we report the structures of two ternary complexes among flagellar chaperones (FliT and FliS), protein substrates (the filament-capping FliD and flagellin FliC), and the export gate platform protein FlhA. The substrates do not interact directly with FlhA; however, they are required to induce a binding-competent conformation to the chaperone that exposes the recognition motif featuring a highly conserved sequence recognized by FlhA. The structural data reveal the recognition signal in a class of T3SS proteins and provide new insight into the assembly of key protein complexes at the export gate.},
doi = {10.1038/s41467-018-04137-4},
journal = {Nature Communications},
number = 1,
volume = 9,
place = {United States},
year = {Wed May 02 00:00:00 EDT 2018},
month = {Wed May 02 00:00:00 EDT 2018}
}
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