Molecular Organization of Soluble Type III Secretion System Sorting Platform Complexes.
Bernal et al.pdf
Microsoft Word 2007
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
Horstmann, Julia A
MetadataShow full item record
AbstractMany medically relevant Gram-negative bacteria use the type III secretion system (T3SS) to translocate effector proteins into the host for their invasion and intracellular survival. A multi-protein complex located at the cytosolic interface of the T3SS is proposed to act as a sorting platform by selecting and targeting substrates for secretion through the system. However, the precise stoichiometry and 3D organization of the sorting platform components are unknown. Here we reconstitute soluble complexes of the Salmonella Typhimurium sorting platform proteins including the ATPase InvC, the regulator OrgB, the protein SpaO and a recently identified subunit SpaOC, which we show to be essential for the solubility of SpaO. We establish domain-domain interactions, determine for the first time the stoichiometry of each subunit within the complexes by native mass spectrometry and gain insight into their organization using small-angle X-ray scattering. Importantly, we find that in solution the assembly of SpaO/SpaOC/OrgB/InvC adopts an extended L-shaped conformation resembling the sorting platform pods seen in in situ cryo-electron tomography, proposing that this complex is the core building block that can be conceivably assembled into higher oligomers to form the T3SS sorting platform. The determined molecular arrangements of the soluble complexes of the sorting platform provide important insights into its architecture and assembly.
CitationJ Mol Biol. 2019 Jul 6. pii: S0022-2836(19)30425-5. doi: 10.1016/j.jmb.2019.07.004.
AffiliationCSSB, Centre for Structural Systembiologie, Notkestr.85, 22607 Hamburg. Germany.
JournalJournal of Molecular Biology
The following license files are associated with this item:
- Role of SpaO in the assembly of the sorting platform of a Salmonella type III secretion system.
- Authors: Lara-Tejero M, Qin Z, Hu B, Butan C, Liu J, Galán JE
- Issue date: 2019 Jan
- Structural analysis of ligand-bound states of the Salmonella type III secretion system ATPase InvC.
- Authors: Bernal I, Römermann J, Flacht L, Lunelli M, Uetrecht C, Kolbe M
- Issue date: 2019 Oct
- The cytoplasmic domain of MxiG interacts with MxiK and directs assembly of the sorting platform in the <i>Shigella</i> type III secretion system.
- Authors: Tachiyama S, Chang Y, Muthuramalingam M, Hu B, Barta ML, Picking WL, Liu J, Picking WD
- Issue date: 2019 Dec 13
- Functional Characterization of EscK (Orf4), a Sorting Platform Component of the Enteropathogenic Escherichia coli Injectisome.
- Authors: Soto E, Espinosa N, Díaz-Guerrero M, Gaytán MO, Puente JL, González-Pedrajo B
- Issue date: 2017 Jan 1
- Visualization of the type III secretion sorting platform of Shigella flexneri.
- Authors: Hu B, Morado DR, Margolin W, Rohde JR, Arizmendi O, Picking WL, Picking WD, Liu J
- Issue date: 2015 Jan 27