2020
DOI: 10.1111/mmi.14658
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Adaptivity and dynamics in type III secretion systems

Abstract: The type III secretion system is the common core of two bacterial molecular machines: the flagellum and the injectisome. The flagellum is the most widely distributed prokaryotic locomotion device, whereas the injectisome is a syringe‐like apparatus for inter‐kingdom protein translocation, which is essential for virulence in important human pathogens. The successful concept of the type III secretion system has been modified for different bacterial needs. It can be adapted to changing conditions, and was found t… Show more

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Cited by 16 publications
(15 citation statements)
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References 227 publications
(339 reference statements)
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“…A sixth protein, FliO, is believed to be required for the assembly of the fT3SScc but does not form part of the complex (Fabiani et al , 2017; Fukumura et al , 2017). The assembly of the fT3SScc initiates with FliP, which forms a pentameric platform on which FliQ, FliR, and FlhB assemble to create a FliP 5 FliQ 4 FliR 1 FlhB 1 subcomplex upon which a nonameric FlhA ring is built (Fabiani et al , 2017; Kuhlen et al , 2018; Minamino et al , 2019; Milne‐Davies et al , 2021). The C‐terminal domains of both FlhA and FlhB remain in the cytoplasm (Fig 1, top).…”
Section: Introductionmentioning
confidence: 99%
“…A sixth protein, FliO, is believed to be required for the assembly of the fT3SScc but does not form part of the complex (Fabiani et al , 2017; Fukumura et al , 2017). The assembly of the fT3SScc initiates with FliP, which forms a pentameric platform on which FliQ, FliR, and FlhB assemble to create a FliP 5 FliQ 4 FliR 1 FlhB 1 subcomplex upon which a nonameric FlhA ring is built (Fabiani et al , 2017; Kuhlen et al , 2018; Minamino et al , 2019; Milne‐Davies et al , 2021). The C‐terminal domains of both FlhA and FlhB remain in the cytoplasm (Fig 1, top).…”
Section: Introductionmentioning
confidence: 99%
“…For Spa33 (SctQ), the dynamic exchange between the sorting platform and cytoplasmic populations is a potential mechanism for guiding secretion cargo to the sorting platform for interaction with Spa47 and Spa13, followed by chaperone removal, unfolding of the cargo and cargo delivery to the export gate. The Yersinia T3SS has yielded seminal findings regarding a dynamic and adaptive network of cytoplasmic and sorting platform-associated proteins [ 141 , 142 ] and there is no reason to suspect that this does not hold true for other T3SS, including that of Shigella . The identification of soluble complexes of the Salmonella sorting platform proteins SpaO, SpaO C , OrgB and InvC (SctQ, SctQ C , SctL and SctN, respectively, or Spa33, Spa33 C , MxiN and Spa47 in Shigella ) is consistent with the stability of such cytoplasmic complexes [ 131 ].…”
Section: The Cytoplasmic Sorting Platform (Bottom)mentioning
confidence: 99%
“…P. mirabilis were grown as described in ref. [4]. P. aeruginosa were grown in LB medium at 37° C overnight.…”
Section: Supporting Information Formentioning
confidence: 99%
“…The fT3SScc consists of five proteins (FliP, FliQ, FliR, FlhB and FlhA), with another protein, FliO, required for assembly but which does not form part of the complex [2,3]. Initially, FliP forms a pentameric platform on which FliQ, FliR and FlhB assemble to create a FliP 5 FliQ 4 FliR 1 FlhB 1 subcomplex upon which an FlhA ring is built [4].…”
mentioning
confidence: 99%