Pilin regulation in the<i>pilT</i>mutant of<i>Neisseria gonorrhoeae</i>strain MS11

Dietrich, Manuela; Mollenkopf, Hans-Joachim; So, Magdalene; Friedrich, Alexandra

doi:10.1111/j.1574-6968.2009.01647.x

Cited by 22 publications

(25 citation statements)

References 40 publications

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“…The PilC protein(s) may operate on a similar principle, allowing an N. gonorrhoeae cell to sense the resistance from neighboring cells tethered to its retracting Tfp and coordinate community and infection behavior through transcriptional reprogramming. In support of this hypothesis, the Δ pilT mutant displays a different transcriptional profile than its wt parent (38). …”

Section: Discussionmentioning

confidence: 81%

“…N. gonorrhoeae pilT L201C grew as well as the wt parent in liquid (data not shown). N. gonorrhoeae Δ pilT is known to be hyperpiliated and to produce significantly higher levels of PilE and pilE mRNA than the wt (2, 38). We found that N. gonorrhoeae pilT L201C transcribed the Tfp-associated genes pilE , pilT , pilT2 , pilU , and pilF at wt levels (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Neisseria gonorrhoeae strains MS11 and MS11 Δ pilT (38) were used throughout this study. All strains were grown on gonococcal broth (GCB) agar plates supplemented with V-C-N (vancomycin, colistin, and nystatin) inhibitor (BBL; BD) or in liquid GCB containing Kellogg’s supplements I and II at 37°C with 5% CO 2 .…”

Section: Methodsmentioning

confidence: 99%

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Attenuation of the Type IV Pilus Retraction Motor Influences Neisseria gonorrhoeae Social and Infection Behavior

Hockenberry

Hutchens

Agellon

et al. 2016

mBio

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Retraction of the type IV pilus (Tfp) mediates DNA uptake, motility, and social and infection behavior in a wide variety of prokaryotes. To date, investigations into Tfp retraction-dependent activities have used a mutant deleted of PilT, the ATPase motor protein that causes the pilus fiber to retract. ΔpilT cells are nontransformable, nonmotile, and cannot aggregate into microcolonies. We tested the hypothesis that these retraction-dependent activities are sensitive to the strength of PilT enzymatic activity by using the pathogen Neisseria gonorrhoeae as a model. We constructed an N. gonorrhoeae mutant with an amino acid substitution in the PilT Walker B box (a substitution of cysteine for leucine at position 201, encoded by pilTL201C). Purified PilTL201C forms a native hexamer, but mutant hexamers hydrolyze ATP at half the maximal rate. N. gonorrhoeae pilTL201C cells produce Tfp fibers, crawl at the same speed as the wild-type (wt) parent, and are equally transformable. However, the social behavior of pilTL201C cells is intermediate between the behaviors of wt and ΔpilT cells. The infection behavior of pilTL201C is also defective, due to its failure to activate the epidermal growth factor receptor (EGFR)-heparin-binding EGF-like growth factor (HB-EGF) pathway. Our study indicates that pilus retraction, per se, is not sufficient for N. gonorrhoeae microcolony formation or infectivity; rather, these activities are sensitive to the strength of PilT enzymatic activity. We discuss the implications of these findings for Neisseria pathogenesis in the context of mechanobiology.

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Section: Discussionmentioning

confidence: 81%

Section: Resultsmentioning

confidence: 99%

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Attenuation of the Type IV Pilus Retraction Motor Influences Neisseria gonorrhoeae Social and Infection Behavior

Hockenberry

Hutchens

Agellon

et al. 2016

mBio

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“…Our data are consistent with observations made in other organisms, such as the cyanobacterium Synechocystis sp. strain PCC6803 and Neisseria gonorrhea, where hyperpiliated pilT mutants have been shown to accumulate higher than normal levels of pilA1 transcript (5,14). One attractive model is that as the pilus is dissembled, PilS senses pilin levels associated with the inner membrane and regulates PilR activity and pilA transcription.…”

Section: Discussionmentioning

confidence: 99%

Genetic Analysis of the Regulation of Type IV Pilus Function by the Chp Chemosensory System of Pseudomonas aeruginosa

2010

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The virulence of the opportunistic pathogen Pseudomonas aeruginosa involves the coordinate expression of many virulence factors, including type IV pili, which are required for colonization of host tissues and for twitching motility. Type IV pilus function is controlled in part by the Chp chemosensory system, which includes a histidine kinase, ChpA, and two CheY-like response regulators, PilG and PilH. How the Chp components interface with the type IV pilus motor proteins PilB, PilT, and PilU is unknown. We present genetic evidence confirming the role of ChpA, PilG, and PilB in the regulation of pilus extension and the role of PilH and PilT in regulating pilus retraction. Using informative double and triple mutants, we show that (i) ChpA, PilG, and PilB function upstream of PilH, PilT, and PilU; (ii) that PilH enhances PilT function; and (iii) that PilT and PilB retain some activity in the absence of signaling input from components of the Chp system. By site-directed mutagenesis, we demonstrate that the histidine kinase domain of ChpA and the phosphoacceptor sites of both PilG and PilH are required for type IV pilus function, suggesting that they form a phosphorelay system important in the regulation of pilus extension and retraction. Finally, we present evidence suggesting that pilA transcription is regulated by intracellular PilA levels. We show that PilA is a negative regulator of pilA transcription in P. aeruginosa and that the Chp system functionally regulates pilA transcription by controlling PilA import and export.

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“…Real-time quantitative reverse transcription-PCR (qRT-PCR), performed as previously described (34), was used to confirm microarray results and analyze expression of the tryptophanase operon, holE, hha, and ydgT. Briefly, 1 g of total RNA was reverse transcribed to generate cDNA using the high-capacity cDNA reverse transcription kit (Applied Biosystems) as recommended by the manufacturer.…”

Section: Methodsmentioning

confidence: 99%

Evidence for Moonlighting Functions of the Subunit of Escherichia coli DNA Polymerase III

Dietrich¹,

Pedró²,

García³

et al. 2013

Journal of Bacteriology

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The holE gene is an enterobacterial ORFan gene (open reading frame [ORF] with no detectable homology to other ORFs in a database). It encodes the subunit of the DNA polymerase III core complex. The precise function of the subunit within this complex is not well established, and loss of holE does not result in a noticeable phenotype. Paralogs of holE are also present on many conjugative plasmids and on phage P1 (hot gene). In this study, we provide evidence indicating that (HolE) exhibits structural and functional similarities to a family of nucleoid-associated regulatory proteins, the Hha/YdgT-like proteins that are also encoded by enterobacterial ORFan genes. Microarray studies comparing the transcriptional profiles of Escherichia coli holE, hha, and ydgT mutants revealed highly similar expression patterns for strains harboring holE and ydgT alleles. Among the genes differentially regulated in both mutants were genes of the tryptophanase (tna) operon. The tna operon consists of a transcribed leader region, tnaL, and two structural genes, tnaA and tnaB. Further experiments with transcriptional lacZ fusions (tnaL::lacZ and tnaA::lacZ) indicate that HolE and YdgT downregulate expression of the tna operon by possibly increasing the level of Rhodependent transcription termination at the tna operon's leader region. Thus, for the first time, a regulatory function can be attributed to HolE, in addition to its role as structural component of the DNA polymerase III complex.

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Pilin regulation in thepilTmutant ofNeisseria gonorrhoeaestrain MS11

Cited by 22 publications

References 40 publications

Attenuation of the Type IV Pilus Retraction Motor Influences Neisseria gonorrhoeae Social and Infection Behavior

Attenuation of the Type IV Pilus Retraction Motor Influences Neisseria gonorrhoeae Social and Infection Behavior

Genetic Analysis of the Regulation of Type IV Pilus Function by the Chp Chemosensory System of Pseudomonas aeruginosa

Evidence for Moonlighting Functions of the Subunit of Escherichia coli DNA Polymerase III

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