Interaction between FliE and FlgB, a Proximal Rod Component of the Flagellar Basal Body of
            <i>Salmonella</i>

Minamino, Tetsuo; Yamaguchi, Shigeru; Macnab, Robert M.

doi:10.1128/jb.182.11.3029-3036.2000

Cited by 77 publications

(74 citation statements)

References 25 publications

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“…These types of interactions are anticipated for the type III secretion system (TTSS), which facilitates delivery of many bacterial effectors from the cytoplasm of gram-negative bacterial pathogens into host cells. Many protein-protein interactions have been demonstrated for the type III-related flagellar assembly apparatus, in terms of both components and substrates interacting with the flagellar assembly apparatus (6,19,23,29,42,44,46,54,61).…”

Section: Few Interactions Have Been Reported Between Effectors and Comentioning

confidence: 99%

Translocated Intimin Receptor and Its Chaperone Interact with ATPase of the Type III Secretion Apparatus of EnteropathogenicEscherichia coli

2003

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Few interactions have been reported between effectors and components of the type III secretion apparatus, although many interactions have been demonstrated between type III effectors and their cognate chaperones.It is thought that chaperones may play a role in directing effectors to the type III secretion apparatus. The ATPase FliI in the flagellar assembly apparatus plays a pivotal role in interacting with other components of the apparatus and with substrates of the flagellar system. We performed experiments to determine if there were any interactions between the effector Tir and its chaperone CesT and the type III secretion apparatus of enteropathogenic Escherichia coli (EPEC). Specifically, based on analogies with the flagella system, we examined Tir-CesT interactions with the putative ATPase EscN. We showed by affinity chromatography that EscN and Tir bind CesT specifically. Tir is not necessary for CesT and EscN interactions, and EscN binds Tir specifically without its chaperone CesT. Moreover, Tir directly binds EscN, as shown via gel overlay and enzyme-linked immunosorbent assay, and coimmunoprecipitation experiments revealed that Tir interacts with EscN inside EPEC. These data provide evidence for direct interactions between a chaperone, effector, and type III component in the pathogenic type III secretion system and suggest a model for Tir translocation whereby its chaperone, CesT, brings Tir to the type III secretion apparatus by specifically interacting with the type III ATPase EscN.Numerous substrates of protein transport systems, ranging from the sec export pathway in bacteria to the mitochondrial import system in eukaryotic cells, interact with components of the transport machinery during transit (37, 51). These types of interactions are anticipated for the type III secretion system (TTSS), which facilitates delivery of many bacterial effectors from the cytoplasm of gram-negative bacterial pathogens into host cells. Many protein-protein interactions have been demonstrated for the type III-related flagellar assembly apparatus, in terms of both components and substrates interacting with the flagellar assembly apparatus (6,19,23,29,42,44,46,54,61).The ATPase FliI in the flagellar assembly apparatus appears to play a pivotal role in interacting with other components of the apparatus and substrates of the system. FliI is required for the export of flagellin and other export substrates (41, 54). The substrates of the flagellar assembly apparatus, such as flagellin and other filament-type substrates, interact with both cytosolic components (ATPase FliI, FliH, and FliJ) and membranebound components (FlhA and FlhB) of the apparatus (44,54,61). FliI is present in the cytoplasm and in association with the inner membrane in Caulobacter crescentus and Salmonella enterica serovar Typhimurium (4, 55). The ATPase activity of S. enterica serovar Typhimurium FliI, localized to the carboxy terminus, is required for flagellar assembly (16,41). FliI also interacts with a number of components of the flagellar export app...

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Section: Few Interactions Have Been Reported Between Effectors and Comentioning

confidence: 99%

Translocated Intimin Receptor and Its Chaperone Interact with ATPase of the Type III Secretion Apparatus of EnteropathogenicEscherichia coli

2003

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“…Of these 22 proteins, six appear to be key components of the rotary motor. An additional protein is likely to function as an adaptor connecting the motor to the axial component (1). Nine more proteins make up the axial component consisting of a rod (drive shaft), hook (universal joint), junction, filament (propeller), and cap.…”

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confidence: 99%

A partial atomic structure for the flagellar hook of Salmonella typhimurium

Shaikh

Thomas

Chen

et al. 2005

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

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The axial proteins of the bacterial flagellum function as a drive shaft, universal joint, and propeller driven by the flagellar rotary motor; they also form the putative protein export channel. The Nand C-terminal sequences of the eight axial proteins were predicted to form interlocking ␣-domains generating an axial tube. We report on an Ϸ1-nm resolution map of the hook from Salmonella typhimurium, which reveals such a tube made from interdigitated, 1-nm rod-like densities similar to those seen in maps of the filament. Atomic models for the two outer domains of the hook subunit were docked into the corresponding outermost features of the map. The N and C termini of the hook subunit fragment are positioned next to each other and face toward the axis of the hook. The placement of these termini would permit the residues missing in the fragment to form the rod-like features that form the core domain of the hook. We also fit the hook atomic model to an Ϸ2-nm resolution map of the hook from Caulobacter crescentus. The hook protein sequence from C. crescentus is largely homologous to that of S. typhimurium except for a large insertion (20 kDa). According to difference maps and our fitting, this insertion is found on the outer surface of the hook, consistent with our modeling of the hook.bacterial chemotaxis ͉ bacterial motility ͉ electron cryomicroscopy T he bacterial flagellum is the organ of motility for many species of bacteria. About 40 genes are needed to assemble the structure; Ϸ22 of the genes contribute structural proteins found in the completed flagellum. Of these 22 proteins, six appear to be key components of the rotary motor. An additional protein is likely to function as an adaptor connecting the motor to the axial component (1). Nine more proteins make up the axial component consisting of a rod (drive shaft), hook (universal joint), junction, filament (propeller), and cap. Two of the remaining proteins make up rings, which serve as a bushing that allows passage of the drive shaft through the cell wall and outer membrane. The rest of the proteins are associated with the flagellar-specific protein export.The rotary motor, powered by the proton-motive gradient across the cell membrane, turns the filament, which converts torque into thrust. The helical hook of the bacterial flagellum acts as a universal joint, allowing the motor to drive the filament off-axis. The hook connects the rod to the hook-filament junction, which in turn is connected to the filament. The hook, which is assembled before the more distal segments of the axial component, plays a role in the assembly of the filament. The flagellar filament elongates by subunit addition at its distal tip (2, 3). Subunits exported by the cell are thought to diffuse along a channel in the hook (and also the rod within the basal body and partially assembled filament). Three-dimensional reconstructions reveal a 3-nm channel running along the axis of the rod (D.R.T., D. G. Morgan, and D.J.D., unpublished data), hook (4), and filament (5), although higher-resolu...

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“…The class 3 promoters transcribe genes whose products are needed late in the assembly process, including the structural components of the filament, the motor force generators, and the chemosensory genes. The 28 protein is required for the transcription of class 3 promoters (31) but prior to HBB completion is tightly associated with anti- 28 factor FlgM (7,30). Thus, the transcription of class 3 promoters is inhibited until completion of the intermediate hook-basal body structure (16).…”

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confidence: 99%

“…The class 2 promoters mediate the transcription of genes whose products are required for the structure and assembly of the hook-basal body (HBB). In addition, two regulatory proteins, flagellum-specific sigma factor 28 (FliA) and its cognate anti-sigma factor, FlgM, are expressed along with hook-basal body genes. The class 3 promoters transcribe genes whose products are needed late in the assembly process, including the structural components of the filament, the motor force generators, and the chemosensory genes.…”

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confidence: 99%

Posttranscriptional Control of the Salmonella enterica Flagellar Hook Protein FlgE

Lee

Hughes

2006

J Bacteriol

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Previous work suggested that the FlgE (flagellar hook subunit) protein in Salmonella enterica serovar Typhimurium was posttranscriptionally regulated in response to the stage of flagellar assembly. Specifically, the FlgE protein could be detected in flagellar mutants defective at the stages of assembly before or after rod assembly but not in rod assembly mutants, yet flgE mRNA levels were unaffected. To elucidate posttranscriptional mechanisms involved in the coupling of flgE gene expression to hook assembly, the RNA sequences at the 5 and 3 ends of the flgE-containing mRNA processed from the large flgBCDEFGHIJKL operon were determined by rapid amplification of cDNA ends, and secretion of the FlgE protein in different flagellar assembly mutant strains was analyzed. The sequences 5 and 3 of the flgE gene where RNA processing occurred was within 15 bases upstream of the flgD stop codon and at bases 145 to 147 downstream of the flgF start codon, respectively. The ribosome binding site of the flgD gene was found to be inhibitory to flgE translation in strains deleted for the upstream flgD gene, unless the region 15 bases upstream of the flgD stop codon was present. Secretion of FlgE into the periplasm was monitored using ␤-lactamase (Bla) fusions as a periplasm-specific reporter, which conferred resistance to ampicillin when FlgE-Bla was secreted into the periplasm. Using this assay, we found that the effect of rod assembly mutants on FlgE levels was due to FlgE turnover in the periplasm and that the FliE rod component protein was required for efficient FlgE-Bla secretion.

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Interaction between FliE and FlgB, a Proximal Rod Component of the Flagellar Basal Body of Salmonella

Cited by 77 publications

References 25 publications

Translocated Intimin Receptor and Its Chaperone Interact with ATPase of the Type III Secretion Apparatus of EnteropathogenicEscherichia coli

Translocated Intimin Receptor and Its Chaperone Interact with ATPase of the Type III Secretion Apparatus of EnteropathogenicEscherichia coli

A partial atomic structure for the flagellar hook of Salmonella typhimurium

Posttranscriptional Control of the Salmonella enterica Flagellar Hook Protein FlgE

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