scholarly journals Hook‐basal body assembly state dictates substrate specificity of the flagellar type‐III secretion system

2021 ◽  
Author(s):  
Alina Guse ◽  
Manuel Halte ◽  
Svenja Hüsing ◽  
Marc Erhardt
Keyword(s):  
Substrate Specificity ◽  
Basal Body ◽  
Type Iii Secretion ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Type Iii

scholarly journals YscP and YscU Regulate Substrate Specificity of the Yersinia Type III Secretion System

2003 ◽  
Vol 185 (7) ◽  
pp. 2259-2266 ◽  
Author(s):  
Petra J. Edqvist ◽  
Jan Olsson ◽  
Moa Lavander ◽  
Lena Sundberg ◽  
Åke Forsberg ◽  
...  
Keyword(s):  
Cell Surface ◽  
Substrate Specificity ◽  
Type Iii Secretion ◽  
Bacterial Cell ◽  
Type Iii Secretion System ◽  
Eukaryotic Cell ◽  
Secretion System ◽  
Cell Contact ◽  
Type Iii ◽  
Bacterial Cell Surface

ABSTRACT Pathogenic Yersinia species use a type III secretion system to inhibit phagocytosis by eukaryotic cells. At 37°C, the secretion system is assembled, forming a needle-like structure on the bacterial cell surface. Upon eukaryotic cell contact, six effector proteins, called Yops, are translocated into the eukaryotic cell cytosol. Here, we show that a yscP mutant exports an increased amount of the needle component YscF to the bacterial cell surface but is unable to efficiently secrete effector Yops. Mutations in the cytoplasmic domain of the inner membrane protein YscU suppress the yscP phenotype by reducing the level of YscF secretion and increasing the level of Yop secretion. These results suggest that YscP and YscU coordinately regulate the substrate specificity of the Yersinia type III secretion system. Furthermore, we show that YscP and YscU act upstream of the cell contact sensor YopN as well as the inner gatekeeper LcrG in the pathway of substrate export regulation. These results further strengthen the strong evolutionary link between flagellar biosynthesis and type III synthesis.

scholarly journals The Structures of SctK and SctD from Pseudomonas aeruginosa Reveal the Interface of the Type III Secretion System Basal Body and Sorting Platform

2020 ◽  
Vol 432 (24) ◽  
pp. 166693
Author(s):  
Meenakumari Muthuramalingam ◽  
Sean K. Whittier ◽  
Scott Lovell ◽  
Kevin P. Battaile ◽  
Shoichi Tachiyama ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Basal Body ◽  
Type Iii Secretion ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Type Iii

scholarly journals YscP and YscU Switch the Substrate Specificity of the Yersinia Type III Secretion System by Regulating Export of the Inner Rod Protein YscI

2008 ◽  
Vol 190 (12) ◽  
pp. 4252-4262 ◽  
Author(s):  
Sarah E. Wood ◽  
Jin Jin ◽  
Scott A. Lloyd
Keyword(s):  
Substrate Specificity ◽  
Type Iii Secretion ◽  
Critical Role ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Eukaryotic Cells ◽  
Bacterial Surface ◽  
Type Iii ◽  
Proper Length ◽  
Null Strain

ABSTRACT Pathogenic yersiniae utilize a type III secretion system to inject antihost factors, called Yops, directly into the cytosol of eukaryotic cells. The Yops are injected via a needle-like structure, comprising the YscF protein, on the bacterial surface. While the needle is being assembled, Yops cannot be secreted. YscP and YscU switch the substrate specificity of the secretion system to enable Yop export once the needle attains its proper length. Here, we demonstrate that the inner rod protein YscI plays a critical role in substrate specificity switching. We show that YscI is secreted by the type III secretion system and that YscI secretion by a yscP mutant is abnormally elevated. Furthermore, we show that mutations in the cytoplasmic domain of YscU reduce YscI secretion by the yscP null strain. We also demonstrate that mutants expressing one of three forms of YscI (those with mutations Q84A, L87A, and L96A) secrete substantial amounts of Yops yet exhibit severe defects in needle formation. In the absence of YscP, mutants with the same changes in YscI assemble needles but are unable to secrete Yops. Together, these results suggest that the formation of the inner rod, not the needle, is critical for substrate specificity switching and that YscP and YscU exert their effects on substrate export by controlling the secretion of YscI.

scholarly journals Structural modeling of the flagellum MS ring protein FliF reveals similarities to the type III secretion system and sporulation complex

PeerJ ◽  
2016 ◽  
Vol 4 ◽  
pp. e1718 ◽  
Author(s):  
Julien R. Bergeron
Keyword(s):  
Basal Body ◽  
Type Iii Secretion ◽  
Bacterial Species ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Primary Role ◽  
Bacterial Surface ◽  
Type Iii ◽  
C Terminus ◽  
Cytosolic Side

The flagellum is a large proteinaceous organelle found at the surface of many bacteria, whose primary role is to allow motility through the rotation of a long extracellular filament. It is an essential virulence factor in many pathogenic species, and is also a priming component in the formation of antibiotic-resistant biofilms. The flagellum consists of the export apparatus on the cytosolic side; the basal body and rotor, spanning the bacterial membrane(s) and periplasm; and the hook-filament, that protrudes away from the bacterial surface. Formation of the basal body MS ring region, constituted of multiple copies of the protein FliF, is one of the initial steps of flagellum assembly. However, the precise architecture of FliF is poorly understood. Here, I report a bioinformatics analysis of the FliF sequence from various bacterial species, suggesting that its periplasmic region is composed of three globular domains. The first two are homologous to that of the type III secretion system injectisome proteins SctJ, and the third possesses a similar fold to that of the sporulation complex component SpoIIIAG. I also describe thatChlamydiapossesses an unusual FliF protein, lacking part of the SctJ homology domain and the SpoIIIAG-like domain, and fused to the rotor component FliG at its C-terminus. Finally, I have combined the sequence analysis of FliF with the EM map of the MS ring, to propose the first atomic model for the FliF oligomer, suggesting that FliF is structurally akin to a fusion of the two injectisome components SctJ and SctD. These results further define the relationship between the flagellum, injectisome and sporulation complex, and will facilitate future structural characterization of the flagellum basal body.

scholarly journals Interplay between predicted inner-rod and gatekeeper in controlling substrate specificity of the type III secretion system

2013 ◽  
Vol 87 (6) ◽  
pp. 1183-1199 ◽  
Author(s):  
Youness Cherradi ◽  
Lionel Schiavolin ◽  
Simon Moussa ◽  
Alaeddine Meghraoui ◽  
Ahmed Meksem ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Type Iii Secretion ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Type Iii

scholarly journals The Modular Structure of the Inner-Membrane Ring Component PrgK Facilitates Assembly of the Type III Secretion System Basal Body

Structure ◽  
2015 ◽  
Vol 23 (1) ◽  
pp. 161-172 ◽  
Author(s):  
Julien R.C. Bergeron ◽  
Liam J. Worrall ◽  
Soumya De ◽  
Nikolaos G. Sgourakis ◽  
Adrienne H. Cheung ◽  
...  
Keyword(s):  
Basal Body ◽  
Type Iii Secretion ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Modular Structure ◽  
Inner Membrane ◽  
Type Iii

scholarly journals Structural modeling of the flagellum MS ring protein FliF reveals similarities to the type III secretion system and sporulation complex

2015 ◽  
Author(s):  
Julien R. C. Bergeron
Keyword(s):  
Basal Body ◽  
Type Iii Secretion ◽  
Structural Model ◽  
Bacterial Species ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Globular Domain ◽  
Primary Role ◽  
Bacterial Flagellum ◽  
Type Iii

The flagellum is a large proteinaceous organelle found at the surface of many bacteria, whose primary role is to allow motility through the rotation of a long extracellular filament. It is an essential virulence factor in many pathogenic species, and is also a priming component in the formation of antibiotic-resistant biofilms. The flagellum consists of the export apparatus and stator in the cytosol; the basal body, spanning the bacterial membrane(s) and periplasm; and the hook-filament, that protrudes away from the bacterial surface. Assembly of the bacterial flagellum is initiated by the formation of the basal body MS ring region, constituted of multiple copies of the protein FliF. Here, I report an analysis of the FliF sequence from various bacterial species, demonstrating that its periplasmic region is composed of a domain homologuous to that of the type III secretion system proteins PrgK, and of a second globular domain that possesses a similar fold to that of the sporulation complex component SpoIIIAG. I also report a structural model for the FliF oligomer, based on knowledge of the PrgK oligomer. These results further emphasize the similarity between the flagellum, T3SS and sporulation complex, and will facilitate further structural studies.

scholarly journals HpaC Controls Substrate Specificity of the Xanthomonas Type III Secretion System

2008 ◽  
Vol 4 (6) ◽  
pp. e1000094 ◽  
Author(s):  
Christian Lorenz ◽  
Steve Schulz ◽  
Thomas Wolsch ◽  
Ombeline Rossier ◽  
Ulla Bonas ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Type Iii Secretion ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Type Iii
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