The assembly of the export apparatus (YscR,S,T,U,V) of the Yersinia type III secretion apparatus occurs independently of other structural components and involves the formation of an YscV oligomer

Diepold, Andreas; Wiesand, Ulrich; Cornelis, Guy R.

doi:10.1111/j.1365-2958.2011.07830.x

Cited by 87 publications

(130 citation statements)

References 97 publications

Supporting

Mentioning

121

Contrasting

Order By: Relevance

“…While studies in Salmonella SPI-1 suggest an insideout assembly of the membrane rings [130 -132], similar to the model for the flagellum, the secretin was shown to nucleate membrane ring assembly in Y. enterocolitica [113], similar to type IV pili [133]. Independently, the export apparatus can assemble within the IM [114,134]. After the concurrent assembly of the cytosolic complex, requiring all of its components SctN, SctL, SctQ and SctL (but not the stalk SctO), the T3SS is functional and the needle can be formed [113,135].…”

Section: Transcription Hierarchy Assembly and Activation Of The T3ssmentioning

confidence: 99%

“…The Salmonella SPI-2 system was found to be present in very low numbers (one to a few [110]), whereas 10-100 SPI-1 needle complexes [111] and 50-100 Shigella needle complexes [112] were observed per bacterium. The distribution of injectisomes was determined by fluorescence microscopy of functional fluorescently labelled components in Yersinia enterocolitica [113,114]. All analysed components were distributed in relatively evenly spaced foci around the bacterium, which is also the case in Shigella [115].…”

Section: What Determines the Number And Cellular Distribution Of T3ss?mentioning

confidence: 99%

See 1 more Smart Citation

Type III secretion systems: the bacterial flagellum and the injectisome

Diepold

Armitage

2015

Phil. Trans. R. Soc. B

Self Cite

184

175

View full text Add to dashboard Cite

One contribution of 12 to a theme issue 'The bacterial cell envelope'. The flagellum and the injectisome are two of the most complex and fascinating bacterial nanomachines. At their core, they share a type III secretion system (T3SS), a transmembrane export complex that forms the extracellular appendages, the flagellar filament and the injectisome needle. Recent advances, combining structural biology, cryo-electron tomography, molecular genetics, in vivo imaging, bioinformatics and biophysics, have greatly increased our understanding of the T3SS, especially the structure of its transmembrane and cytosolic components, the transcriptional, post-transcriptional and functional regulation and the remarkable adaptivity of the system. This review aims to integrate these new findings into our current knowledge of the evolution, function, regulation and dynamics of the T3SS, and to highlight commonalities and differences between the two systems, as well as their potential applications.

show abstract

Section: Transcription Hierarchy Assembly and Activation Of The T3ssmentioning

confidence: 99%

Section: What Determines the Number And Cellular Distribution Of T3ss?mentioning

confidence: 99%

Type III secretion systems: the bacterial flagellum and the injectisome

Diepold

Armitage

2015

Phil. Trans. R. Soc. B

Self Cite

184

175

View full text Add to dashboard Cite

show abstract

“…It is therefore conceivable that ring formation is a common characteristic of IM-and OM-associated components of the T3S sys- tem. Notably, YscV and its flagellar homolog FlhA were reported to oligomerize, and it was assumed that approximately 20 subunits of FlhA are incorporated into the flagellar export apparatus, where they might form a ring structure outside the MS ring (143,316). In future studies, it remains to be investigated whether the assembly of the export apparatus in the IM does indeed involve the formation of ring structures.…”

Section: The Im Ring Components Of Translocation-associated and Flagementioning

confidence: 99%

Protein Export According to Schedule: Architecture, Assembly, and Regulation of Type III Secretion Systems from Plant- and Animal-Pathogenic Bacteria

Büttner

2012

Microbiol Mol Biol Rev

363

482

View full text Add to dashboard Cite

SUMMARY Flagellar and translocation-associated type III secretion (T3S) systems are present in most Gram-negative plant- and animal-pathogenic bacteria and are often essential for bacterial motility or pathogenicity. The architectures of the complex membrane-spanning secretion apparatuses of both systems are similar, but they are associated with different extracellular appendages, including the flagellar hook and filament or the needle/pilus structures of translocation-associated T3S systems. The needle/pilus is connected to a bacterial translocon that is inserted into the host plasma membrane and mediates the transkingdom transport of bacterial effector proteins into eukaryotic cells. During the last 3 to 5 years, significant progress has been made in the characterization of membrane-associated core components and extracellular structures of T3S systems. Furthermore, transcriptional and posttranscriptional regulators that control T3S gene expression and substrate specificity have been described. Given the architecture of the T3S system, it is assumed that extracellular components of the secretion apparatus are secreted prior to effector proteins, suggesting that there is a hierarchy in T3S. The aim of this review is to summarize our current knowledge of T3S system components and associated control proteins from both plant- and animal-pathogenic bacteria.

show abstract

“…Assembly of the needle complex is a coordinated process, which in the S. Typhimurium SPI-1-encoded TTSS is initiated by a subset of membrane proteins (SpaP, SpaQ, SpaR, and SpaS) that are thought to form a protein channel in the inner membrane (13,14). The inner rings of the base assemble around these membrane proteins and after addition of the independently assembled outer rings, the base substructure becomes competent for type III secretion (13,15). However, the base substructure has very narrow substrate specificity because it can only recognize the inner rod (PrgJ) and needle (PrgI) protein subunits and a regulatory protein (InvJ).…”

mentioning

confidence: 99%

The inner rod protein controls substrate switching and needle length in a Salmonella type III secretion system

Lefebre

Galán

2013

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Type III secretion machines are essential for the biology of many bacteria that are pathogenic or symbiotic for animals, plants, or insects. They exert their function by delivering bacterial effector proteins into target eukaryotic cells. The core component of these machines is the needle complex, a multiprotein structure that spans the bacterial envelope and serves as a conduit for proteins that transit this secretion pathway. The needle complex is composed of a multiring base embedded in the bacterial envelope and a filament-like structure, the needle, that projects from the bacterial surface and is linked to the base by the inner rod. Assembly of the needle complex proceeds in a step-wise fashion that is initiated by the assembly of the base and is followed by the export of the building subunits for the needle and inner rod substructures. Once assembled, the needle complex reprograms its specificity and becomes competent for the secretion of effector proteins. Here through genetic, biochemical, and electron microscopy analyses of the Salmonella inner rod protein subunit PrgJ we present evidence that the assembly of the inner rod dictates the timing of substrate switching and needle length. Furthermore, the identification of mutations in PrgJ that specifically alter the hierarchy of protein secretion provides additional support for a complex role of the inner rod substructure in type III secretion.bacterial pathogenesis | organelle assembly | Salmonella pathogenesis

show abstract

The assembly of the export apparatus (YscR,S,T,U,V) of the Yersinia type III secretion apparatus occurs independently of other structural components and involves the formation of an YscV oligomer

Cited by 87 publications

References 97 publications

Type III secretion systems: the bacterial flagellum and the injectisome

Type III secretion systems: the bacterial flagellum and the injectisome

Protein Export According to Schedule: Architecture, Assembly, and Regulation of Type III Secretion Systems from Plant- and Animal-Pathogenic Bacteria

The inner rod protein controls substrate switching and needle length in a Salmonella type III secretion system

Contact Info

Product

Resources

About