FlhF and Its GTPase Activity Are Required for Distinct Processes in Flagellar Gene Regulation and Biosynthesis in
            <i>Campylobacter jejuni</i>

Balaban, Murat Ö.; Joslin, Stephanie N.; Hendrixson, David R.

doi:10.1128/jb.00884-09

Cited by 65 publications

(112 citation statements)

References 49 publications

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“…The blots were then developed using Western Blue Stabilized Substrate (Promega). For anti-FlgG, nitrocellulose membranes were blocked using 2.5% BSA and probed with 1:1,000 dilution of mouse anti-FlgG M69 antibody (gift from Hendrixson, DR) (23). To visualize, the membranes were then blotted with rabbit anti-mouse IgG secondary antibody conjugated to horseradish peroxidase (1:10,000) (GE Healthcare) and developed using the ECL plus Western blotting detection system (GE Healthcare).…”

Section: Modification Of Flagellar Rod Protein Flgg By C Jejunimentioning

confidence: 99%

Characterization of Unique Modification of Flagellar Rod Protein FlgG by Campylobacter jejuni Lipid A Phosphoethanolamine Transferase, Linking Bacterial Locomotion and Antimicrobial Peptide Resistance

Cullen

Madsen

Ivanov

et al. 2012

Journal of Biological Chemistry

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Background: C. jejuni modify the flagellar protein FlgG and lipid A with phosphoethanolamine. Results: The C. jejuni phosphoethanolamine transferase EptC modifies FlgG at position Thr 75 . Conclusion: Phosphoethanolamine modification of FlgG is required for motility, whereas modification of lipid A with phosphoethanolamine results in resistance to antimicrobial peptides. Significance: Understanding how bacterial surface modifications influence and regulate virulence is key for the development of novel therapeutics.

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Section: Modification Of Flagellar Rod Protein Flgg By C Jejunimentioning

confidence: 99%

Characterization of Unique Modification of Flagellar Rod Protein FlgG by Campylobacter jejuni Lipid A Phosphoethanolamine Transferase, Linking Bacterial Locomotion and Antimicrobial Peptide Resistance

Cullen

Madsen

Ivanov

et al. 2012

Journal of Biological Chemistry

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“…In contrast to C. jejuni flgS or T3SS mutants, these partially FlgS-and T3SS-independent FlgR mutant proteins do not suppress the phenotype of an flhF deletion mutant for expression of 54 -dependent flagellar genes (40). In addition, a double mutant lacking flhF and a secretory apparatus is more defective for expression of 54 -dependent flagellar genes than either single mutant.…”

Section: Transcriptional Regulatory Cascades For Flagellar Gene Exprementioning

confidence: 77%

“…1). Strong evidence from C. jejuni supports a model in which the T3SS influences activation of the FlgSR system, with the FlhF GTPase functioning possibly outside and downstream of this pathway for full expression of the 54 regulon (40,255,300 54 -dependent expression of flagellar genes (300,301).…”

Section: Transcriptional Regulatory Cascades For Flagellar Gene Exprementioning

confidence: 78%

“…Current hypotheses propose that FlhF may function downstream of or converge with the T3SS-FlgSR pathway to activate 54 . Further analysis of FlhF demonstrated that full GTPase activity of FlhF is not required for expression of 54 -dependent flagellar genes (40). Mechanistic details regarding how FlhF influences activation of expression of 54 -dependent genes in a GTPaseindependent manner remain to be elucidated.…”

Section: Transcriptional Regulatory Cascades For Flagellar Gene Exprementioning

confidence: 99%

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Change Is Good: Variations in Common Biological Mechanisms in the Epsilonproteobacterial GeneraCampylobacterandHelicobacter

Gilbreath

Cody

Merrell

et al. 2011

Microbiol Mol Biol Rev

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SUMMARY Microbial evolution and subsequent species diversification enable bacterial organisms to perform common biological processes by a variety of means. The epsilonproteobacteria are a diverse class of prokaryotes that thrive in diverse habitats. Many of these environmental niches are labeled as extreme, whereas other niches include various sites within human, animal, and insect hosts. Some epsilonproteobacteria, such as Campylobacter jejuni and Helicobacter pylori , are common pathogens of humans that inhabit specific regions of the gastrointestinal tract. As such, the biological processes of pathogenic Campylobacter and Helicobacter spp. are often modeled after those of common enteric pathogens such as Salmonella spp. and Escherichia coli . While many exquisite biological mechanisms involving biochemical processes, genetic regulatory pathways, and pathogenesis of disease have been elucidated from studies of Salmonella spp. and E. coli , these paradigms often do not apply to the same processes in the epsilonproteobacteria. Instead, these bacteria often display extensive variation in common biological mechanisms relative to those of other prototypical bacteria. In this review, five biological processes of commonly studied model bacterial species are compared to those of the epsilonproteobacteria C. jejuni and H. pylori . Distinct differences in the processes of flagellar biosynthesis, DNA uptake and recombination, iron homeostasis, interaction with epithelial cells, and protein glycosylation are highlighted. Collectively, these studies support a broader view of the vast repertoire of biological mechanisms employed by bacteria and suggest that future studies of the epsilonproteobacteria will continue to provide novel and interesting information regarding prokaryotic cellular biology.

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“…The FlhF GTPase of vibrios, pseudomonads, and Campylobacter jejuni may function akin to the TipF and c-di-GMP-dependent flagellar polarization pathway (Pandza et al 2000;Salvetti et al 2007;Balaban et al 2009;Kusumoto et al 2009). FlhF is polarized and recruits the MS ring protein FliF to the polar site of flagellation in Vibrio.…”

Section: Discussionmentioning

confidence: 99%

De- and repolarization mechanism of flagellar morphogenesis during a bacterial cell cycle

et al. 2013

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Eukaryotic morphogenesis is seeded with the establishment and subsequent amplification of polarity cues at key times during the cell cycle, often using (cyclic) nucleotide signals. We discovered that flagellum de-and repolarization in the model prokaryote Caulobacter crescentus is precisely orchestrated through at least three spatiotemporal mechanisms integrated at TipF. We show that TipF is a cell cycle-regulated receptor for the second messenger-bis-(39-59)-cyclic dimeric guanosine monophosphate (c-di-GMP)-that perceives and transduces this signal through the degenerate c-di-GMP phosphodiesterase (EAL) domain to nucleate polar flagellum biogenesis. Once c-di-GMP levels rise at the G1 / S transition, TipF is activated, stabilized, and polarized, enabling the recruitment of downstream effectors, including flagellar switch proteins and the PflI positioning factor, at a preselected pole harboring the TipN landmark. These c-di-GMP-dependent events are coordinated with the onset of tipF transcription in early S phase and together enable the correct establishment and robust amplification of TipF-dependent polarization early in the cell cycle. Importantly, these mechanisms also govern the timely removal of TipF at cell division coincident with the drop in c-di-GMP levels, thereby resetting the flagellar polarization state in the next cell cycle after a preprogrammed period during which motility must be suspended.

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FlhF and Its GTPase Activity Are Required for Distinct Processes in Flagellar Gene Regulation and Biosynthesis in Campylobacter jejuni

Cited by 65 publications

References 49 publications

Characterization of Unique Modification of Flagellar Rod Protein FlgG by Campylobacter jejuni Lipid A Phosphoethanolamine Transferase, Linking Bacterial Locomotion and Antimicrobial Peptide Resistance

Characterization of Unique Modification of Flagellar Rod Protein FlgG by Campylobacter jejuni Lipid A Phosphoethanolamine Transferase, Linking Bacterial Locomotion and Antimicrobial Peptide Resistance

Change Is Good: Variations in Common Biological Mechanisms in the Epsilonproteobacterial GeneraCampylobacterandHelicobacter

De- and repolarization mechanism of flagellar morphogenesis during a bacterial cell cycle

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