Type III Protein Translocase

Pozidis, Charalambos; Chalkiadaki, Aggeliki; Gomez-Serrano, Amalia; Stahlberg, Henning; Brown, Ian R.; Tampakaki, Anastasia P.; Lustig, Ariel; Sianidis, Giorgos; Politou, Anastasia S.; Engel, Andréas; Panopoulos, Nickolas J.; Mansfıeld, John W.; Pugsley, Anthony P.; Karamanou, Spyridoula; Economou, Anastassios

doi:10.1074/jbc.m301903200

Cited by 62 publications

(21 citation statements)

References 47 publications

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“…Mutation of active site residues in the C-terminal domain of FliI are dominant negative for swarming motility (16 -18). Similar studies on the homologous InvC type III ATPase also demonstrated negative dominance of catalytic site mutations that were relieved on disruption of membrane localization of the ATPase (20,21).…”

mentioning

confidence: 62%

Molecular Basis of the Interaction between the Flagellar Export Proteins FliI and FliH from Helicobacter pylori

Lane

O’Toole

Moore

2006

Journal of Biological Chemistry

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Bacterial flagellar protein export requires an ATPase, FliI, and presumptive inhibitor, FliH. We have explored the molecular basis for FliI/FliH interaction in the human gastric pathogen Helicobacter pylori. By using bioinformatic and biochemical analyses, we showed that residues 1-18 of FliI very likely form an amphipathic ␣-helix upon interaction with FliH, and that residues 21-91 of FliI resemble the N-terminal oligomerization domain of the F 1 -ATPase catalytic subunits. A truncated FliI-(2-91) protein was shown to be folded, although the N-terminal 18 residues were likely unstructured. Deletion and scanning mutagenesis showed that residues 1-18 of FliI were essential for the FliI/FliH interaction. Scanning mutation of amino acids in the N-terminal 10 residues of FliI indicated that a cluster of hydrophobic residues in this segment was critical for the interaction with FliH. The interaction between FliI and FliH has similarities to the interaction between the N-terminal ␣-helix of the F 1 -ATPase ␣-subunit and the globular domain of the F 1 -ATPase ␦-subunit, respectively. This similarity suggests that FliH may function as a molecular stator.

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mentioning

confidence: 62%

Molecular Basis of the Interaction between the Flagellar Export Proteins FliI and FliH from Helicobacter pylori

Lane

O’Toole

Moore

2006

Journal of Biological Chemistry

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“…The specific activity increases with an increase in the enzyme concentration until a maximal activity of 50 nmol/ min/mg. Concentration-dependent activity is suggestive of cooperative association and has been identified for a number of characterized NTPases, including AAA-ATPases (34).…”

Section: Resultsmentioning

confidence: 99%

Characterization of Rv3868, an Essential Hypothetical Protein of the ESX-1 Secretion System in Mycobacterium tuberculosis

Luthra

Mahmood

Arora

et al. 2008

Journal of Biological Chemistry

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Rv3868, a conserved hypothetical protein of the ESAT-6 secretion system of Mycobacterium tuberculosis, is essential for the secretion of at least four virulence factors. Each protein chain is ϳ63 kDa and assembles into a hexamer. Limited proteolysis demonstrates that it consists of two domains joined by a linker. The N-terminal domain is a compact, helical domain of ϳ30 kDa and apparently functions to regulate the ATPase activity of the C-terminal domain and the oligomerization. The nucleotide binding site is situated in the C-terminal domain, which exhibits ATP-dependent self-association. It is also the oligomerization domain. Dynamic fluorescence quenching studies demonstrate that the domain is proximal to the C terminus in the apoprotein and exhibits a specific movement upon ATP binding. In silico modeling of the domains suggests that Arg-429 of a neighboring subunit forms a part of the binding site upon oligomerization. Mutational analysis of binding site residues demonstrates that the Arg-429 functions as the important "sensor arginine" in AAA-ATPases. Protein NMR experiments involving CFP-10 and activity assays rule out a general chaperone-like function for Rv3868. On the other hand, ATP-dependent "open-close" movements of the individual domains apparently enable it to interact and transfer energy to co-proteins in the ESX-1 pathway.

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“…4), appears to be an integral membrane protein. To further characterize CtsP and CtsX as integral or peripheral membrane proteins, we analyzed the avidity of their association with C. jejuni membranes by employing different extraction procedures commonly used to release peripherally associated membrane proteins (43).…”

Section: The Walker Boxes Of Ctse and Ctsp Are Required For Function mentioning

confidence: 99%

Characterization and Localization of the Campylobacter jejuni Transformation System Proteins CtsE, CtsP, and CtsX

Beauchamp¹,

Erfurt²,

DiRita³

2014

J. Bacteriol.

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The human pathogen Campylobacter jejuni is naturally competent for transformation with its own DNA. Genes required for efficient transformation in C. jejuni include those similar to components of type II secretion systems found in many Gram-negative bacteria (R. S T he Gram-negative bacterium Campylobacter jejuni is a leading cause of bacterial gastroenteritis worldwide (1). C. jejuni often colonizes the avian intestinal tract; consequently, a common route of infection is through consumption of contaminated poultry (2).A number of Campylobacter species are naturally competent for transformation, meaning that they can take up macromolecular DNA from the environment and incorporate it heritably into their genomes (3, 4). The ability to acquire DNA from the environment may contribute to the extensive genetic diversity observed among strains of C. jejuni (5, 6). Horizontal gene transfer in vivo has been demonstrated during experimental infection of chicks, a natural host for this pathogen (7).Multiple genes whose products are involved in natural transformation of C. jejuni have been identified (8-12). Using transposon mutagenesis and a genetic screen for loss of competence, we isolated mutations that mapped to 11 genes encoded in C. jejuni strain 81-176 (8). Mutations in these result in a reduction in transformability to levels 4 orders of magnitude below the levels seen with the wild type (8). Among these are six genes arranged in a likely operon, some of which encode proteins similar to components of type II secretion and type IV pilus biogenesis systems and homologous to proteins important for natural transformation in other organisms (13). Two of these, ctsE and ctsP, encode putative nucleoside triphosphatases (NTPases) or nucleoside triphosphate (NTP) binding proteins, according to the annotated genome of C. jejuni strain 11168 (8,14).CtsE is a member of the type II secretion/type IV secretion system superfamily of NTPases collectively referred to as the PulE-VirB11 family (15, 16). Members of this family are involved in diverse processes, including secretion, pilus biogenesis, competence for natural transformation, and conjugation (15). PulE-VirB11 family members share several elements, including the nucleotide-binding motifs-Walker boxes A and B-an Asp box, and a His box (17)(18)(19). CtsE also has a tetracysteine motif conserved among the GspE and PilB/HofB subfamilies (20,21).ATPase activity has been demonstrated in vitro for several members of the PulE-VirB11 family (22-26). It is hypothesized that this activity powers the transformation process, though this has yet to be conclusively shown.

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Type III Protein Translocase

Cited by 62 publications

References 47 publications

Molecular Basis of the Interaction between the Flagellar Export Proteins FliI and FliH from Helicobacter pylori

Molecular Basis of the Interaction between the Flagellar Export Proteins FliI and FliH from Helicobacter pylori

Characterization of Rv3868, an Essential Hypothetical Protein of the ESX-1 Secretion System in Mycobacterium tuberculosis

Characterization and Localization of the Campylobacter jejuni Transformation System Proteins CtsE, CtsP, and CtsX

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