Correction: Corrigendum: A simple and versatile design concept for fluorophore derivatives with intramolecular photostabilization

Velde, Jasper H. M. van der; Oelerich, Jens; Huang, Jingyi; Smit, Jochem H.; Jazi, Atieh Aminian; Galiani, Silvia; Kolmakov, Kirill; Gouridis, Giorgos; Eggeling, Christian; Herrmann, Andreas; Roelfes, Gérard; Cordes, Thorben

doi:10.1038/ncomms16144

Nat Commun

2017

DOI: 10.1038/ncomms16144

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Correction: Corrigendum: A simple and versatile design concept for fluorophore derivatives with intramolecular photostabilization

Jasper H. M. van der Velde¹,

Jens Oelerich²,

Jingyi Huang³

et al.

Abstract: Nature Communications 7 Article number: 10144 (2016) Published: 11 January 2016; Updated: 04 August 2017 The original version of this Article contained an error in the spelling of the author Giorgos Gouridis which was incorrectly given as Giorgos Guoridis. This has now been corrected in both the PDFand HTML versions of the Article.

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Structural dynamics of the functional nonameric Type III translocase export gate

Yuan

Portaliou

Parakra

et al. 2020

Preprint

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The Type III protein secretion (T3S) pathway is widespread in bacterial Gram-negative pathogens. It comprises the injectisome with a cytoplasm-facing inner membrane translocase and a surface-exposed needle. The translocase comprises a conical SctR5S4T1 export channel, decorated by SctU, and enveloped by SctV. The large cytoplasmic domain (C-domain) of SctV binds T3S chaperone/exported protein and forms a putative ante-chamber leading to the membrane translocase. Here we probed the mechanism of assembly and function of SctV. Using live cell imaging, SctV was shown to assemble in peripheral oligomeric clusters in both EPEC and a non-T3SS harbouring E.coli strain. Non-ionic detergents extracted SctV homo-nonamers from membranes of both strains. His-SctV9 reconstituted in peptidiscs revealed an elongated, tripartite particle of ~22nm with a membrane domain and a narrower linker connecting to a C-domain. The C-domain assembles in a hollow asymmetric ring with a 5-6 nm-wide inner opening. SctV9 is necessary and sufficient to act as a receptor for two different chaperone/exported protein pairs by binding them at distinct C-domain sites identified by immobilized peptide arrays. Binding sites are not only important for binding but also essential for secretion suggesting a close mechanistic link between the receptor and secretion activities. These findings advance structural understanding of injectisome assembly and reveal that chaperone/exported protein targeting is mechanistically uncoupled from the succeeding translocation step.Author summaryThe export apparatus of the Type III secretion pathway is conserved in flagellar and virulence injectisomes. Its major component SctV, is essential for T3S substrate targeting and translocation. Here, we analysed SctV assembly and function as a receptor for targeting T3S exported proteins. SctV was shown to self-nonamerize, in a structure that is sufficient for functional binding of chaperone/exported protein complexes. Nonameric SctV reconstituted in peptidiscs and its nonameric ring-forming cytoplasmic domain reveal structural features and lay the foundation for high-resolution cryoEM. These tools set the stage for mechanistic dissection of the structural interactions of the export apparatus with the exported proteins, independently of the transmembrane crossing reaction.

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Structural dynamics of the functional nonameric Type III translocase export gate

Yuan

Portaliou

Parakra

et al. 2020

Preprint

Self Cite

View full text Add to dashboard Cite

show abstract

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Correction: Corrigendum: A simple and versatile design concept for fluorophore derivatives with intramolecular photostabilization

Cited by 1 publication

References 0 publications

Structural dynamics of the functional nonameric Type III translocase export gate

Structural dynamics of the functional nonameric Type III translocase export gate

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