Histidine-containing Phosphotransfer Protein-B (HptB) Regulates Swarming Motility through Partner-switching System in Pseudomonas aeruginosa PAO1 Strain

Bhuwan, Manish; Lee, Hui-Ju; Peng, Hwei-Ling; Chang, Hwan‐You

doi:10.1074/jbc.m111.256586

Cited by 45 publications

(81 citation statements)

References 52 publications

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“…These results imply that HsbA has another major regulatory effect on denitrification. Indeed, it was reported that deletion of hsbA and site-directed mutagenesis to simulate constitutive activation of HsbA shared a hyperswarming phenotype (54). This is likely due to other regulatory effects that are not yet understood.…”

Section: Resultsmentioning

confidence: 99%

“…One of these, Psest_1724 (hsbA) (w nitrate ϭ Ϫ1.6 [see Table S3 in the supplemental material]), had the largest w 9 nM MoϪreplete value (2.5) (see Table S4) of any gene and is annotated as an anti-sigma factor antagonist. In P. aeruginosa, HsbA binds the anti-sigma factor FlgM, thereby freeing sigma factor 28, FliA, to facilitate transcription of flagellar and other motility-related genes (54,55). RCH2 has two fliA homologs, Psest_1740 (fliA1) and Psest_4160 (fliA2), with 82% and 38% sequence identity, respectively.…”

Section: Resultsmentioning

confidence: 99%

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Determining Roles of Accessory Genes in Denitrification by Mutant Fitness Analyses

Vaccaro

Thorgersen

Lancaster

et al. 2016

Appl Environ Microbiol

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Enzymes of the denitrification pathway play an important role in the global nitrogen cycle, including release of nitrous oxide, an ozone-depleting greenhouse gas. In addition, nitric oxide reductase, maturation factors, and proteins associated with nitric oxide detoxification are used by pathogens to combat nitric oxide release by host immune systems. While the core reductases that catalyze the conversion of nitrate to dinitrogen are well understood at a mechanistic level, there are many peripheral proteins required for denitrification whose basic function is unclear. A bar-coded transposon DNA library from Pseudomonas stutzeri strain RCH2 was grown under denitrifying conditions, using nitrate or nitrite as an electron acceptor, and also under molybdenum limitation conditions, with nitrate as the electron acceptor. Analysis of sequencing results from these growths yielded gene fitness data for 3,307 of the 4,265 protein-encoding genes present in strain RCH2. The insights presented here contribute to our understanding of how peripheral proteins contribute to a fully functioning denitrification pathway. We propose a new low-affinity molybdate transporter, OatABC, and show that differential regulation is observed for two MoaA homologs involved in molybdenum cofactor biosynthesis. We also propose that NnrS may function as a membrane-bound NO sensor. The dominant HemN paralog involved in heme biosynthesis is identified, and a CheR homolog is proposed to function in nitrate chemotaxis. In addition, new insights are provided into nitrite reductase redundancy, nitric oxide reductase maturation, nitrous oxide reductase maturation, and regulation.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Determining Roles of Accessory Genes in Denitrification by Mutant Fitness Analyses

Vaccaro

Thorgersen

Lancaster

et al. 2016

Appl Environ Microbiol

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“…The hptB gene encodes a histidine phosphotransfer protein involved in a complex regulatory cascade (47)(48)(49). The ⌬hptB mutant of P. aeruginosa PAK has been demonstrated to produce hyperbiofilms and to show elevated Pel polysaccharide production and elevated c-di-GMP levels (48,50).…”

Section: Resultsmentioning

confidence: 99%

PilZ Domain Protein FlgZ Mediates Cyclic Di-GMP-Dependent Swarming Motility Control in Pseudomonas aeruginosa

et al. 2016

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The second messenger cyclic diguanylate (c-di-GMP) is an important regulator of motility in many bacterial species. In Pseudomonas aeruginosa, elevated levels of c-di-GMP promote biofilm formation and repress flagellum-driven swarming motility. The rotation of P. aeruginosa's polar flagellum is controlled by two distinct stator complexes, MotAB, which cannot support swarming motility, and MotCD, which promotes swarming motility. Here we show that when c-di-GMP levels are elevated, swarming motility is repressed by the PilZ domain-containing protein FlgZ and by Pel polysaccharide production. We demonstrate that FlgZ interacts specifically with the motility-promoting stator protein MotC in a c-di-GMP-dependent manner and that a functional green fluorescent protein (GFP)-FlgZ fusion protein shows significantly reduced polar localization in a strain lacking the MotCD stator. Our results establish FlgZ as a c-di-GMP receptor affecting swarming motility by P. aeruginosa and support a model wherein c-di-GMP-bound FlgZ impedes motility via its interaction with the MotCD stator. IMPORTANCEThe regulation of surface-associated motility plays an important role in bacterial surface colonization and biofilm formation. c-di-GMP signaling is a widespread means of controlling bacterial motility, and yet the mechanism whereby this signal controls surface-associated motility in P. aeruginosa remains poorly understood. Here we identify a PilZ domain-containing c-di-GMP effector protein that contributes to c-di-GMP-mediated repression of swarming motility by P. aeruginosa. We provide evidence that this effector, FlgZ, impacts swarming motility via its interactions with flagellar stator protein MotC. Thus, we propose a new mechanism for c-di-GMP-mediated regulation of motility for a bacterium with two flagellar stator sets, increasing our understanding of surface-associated behaviors, a key prerequisite to identifying ways to control the formation of biofilm communities. Cyclic diguanylate (c-di-GMP) is a ubiquitous bacterial second messenger responsible for regulating a range of cellular processes, including motility and biofilm formation (1). In general, low intracellular c-di-GMP levels are associated with motile lifestyles, while elevated levels of c-di-GMP promote surface attachment and sessile lifestyles (2, 3). c-di-GMP is synthesized from two molecules of GTP by diguanylate cyclases (DGCs) and degraded by c-di-GMP-specific phosphodiesterases (PDEs) (1, 4). Many DGCs and PDEs involved in motility regulation have been characterized, but the mechanisms by which c-di-GMP regulates motility are poorly understood in Pseudomonas aeruginosa and in other bacterial species.To regulate numerous biological functions, c-di-GMP binds to specific effector proteins or RNA (reviewed in reference 5). Recent studies have focused on identifying these c-di-GMP effectors and their mechanisms for regulating c-di-GMP-dependent processes. One class of effectors is the PilZ domain-containing protein family, which is characterized by conserved ...

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“…Indeed, this protein consists of three domains: a receiver domain at its N-terminal part (CrsR D1 ), a PP2C-like serine phosphatase domain (CrsR D2 ), and an anti-sigma-like serine kinase domain (CrsR D3 ) (Fig. 1B) (36,41,42). CrsR D2 shows sequence similarity to proteins or protein domains with phosphatase activity like RsbU from B. subtilis, SypE from V. fisheri, and HsbR from P. aeruginosa (Table 1 and Fig.…”

Section: S Oneidensis Genome Contains Amentioning

confidence: 99%

“…However, in these bacteria it has not been shown that these systems are involved in the direct regulation of sigma factors. BtrWVU may post-translationally control the type III secretion system, whereas SypEA promotes biofilm formation by an unknown mechanism, with HsbRA regulating swarming motility (32)(33)(34)(35)(36)(37).…”

mentioning

confidence: 99%

The General Stress Response σS Is Regulated by a Partner Switch in the Gram-negative Bacterium Shewanella oneidensis

Bouillet¹,

Genest²,

Jourlin-Castelli³

et al. 2016

Journal of Biological Chemistry

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Edited by Thomas SöllnerHere, we show that a partner-switching system of the aquatic Proteobacterium Shewanella oneidensis regulates post-translationally S (also called RpoS), the general stress response sigma factor. Genes SO2118 and SO2119 encode CrsA and CrsR, respectively. CrsR is a three-domain protein comprising a receiver, a phosphatase, and a kinase/anti-sigma domains, and CrsA is an anti-sigma antagonist. In vitro, CrsR sequesters S and possesses kinase and phosphatase activities toward CrsA. In turn, dephosphorylated CrsA binds the anti-sigma domain of CrsR to allow the release of S . This study reveals a novel pathway that post-translationally regulates the general stress response sigma factor differently than what was described for other proteobacteria like Escherichia coli. We argue that this pathway allows probably a rapid bacterial adaptation.

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Histidine-containing Phosphotransfer Protein-B (HptB) Regulates Swarming Motility through Partner-switching System in Pseudomonas aeruginosa PAO1 Strain

Cited by 45 publications

References 52 publications

Determining Roles of Accessory Genes in Denitrification by Mutant Fitness Analyses

Determining Roles of Accessory Genes in Denitrification by Mutant Fitness Analyses

PilZ Domain Protein FlgZ Mediates Cyclic Di-GMP-Dependent Swarming Motility Control in Pseudomonas aeruginosa

The General Stress Response σS Is Regulated by a Partner Switch in the Gram-negative Bacterium Shewanella oneidensis

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