scholarly journals GsmR, a response regulator with an HD-related output domain inXanthomonas campestris, is positively controlled by Clp and is involved in the expression of genes responsible for flagellum synthesis

FEBS Journal ◽  
2012 ◽  
Vol 280 (1) ◽  
pp. 199-213 ◽  
Author(s):  
Yu-Fan Liu ◽  
Chao-Tsai Liao ◽  
Wan-Ling Song ◽  
Pei-Chi Hsu ◽  
Shin-Chiao Du ◽  
...  
Keyword(s):  
Response Regulator ◽  
Expression Of Genes ◽  
Output Domain

scholarly journals Photo sensing and quorum sensing are integrated to control bacterial group behaviors

2019 ◽  
Author(s):  
Sampriti Mukherjee ◽  
Matthew Jemielita ◽  
Vasiliki Stergioula ◽  
Mikhail Tikhonov ◽  
Bonnie L. Bassler
Keyword(s):  
Quorum Sensing ◽  
Biofilm Formation ◽  
Response Regulator ◽  
Sensory Information ◽  
Virulence Gene ◽  
Component System ◽  
Virulence Gene Expression ◽  
Bacterial Phyla ◽  
Expression Of Genes ◽  
Genes Encoding

ABSTRACTPseudomonas aeruginosa transitions between the free-swimming state and the sessile biofilm mode during its pathogenic lifestyle. We show that quorum sensing represses P. aeruginosa biofilm formation and virulence by activating expression of genes encoding the KinB-AlgB two-component system. Phospho-AlgB represses biofilm and virulence genes, while KinB dephosphorylates, and thereby, inactivates AlgB. We discover that the photoreceptor BphP is the kinase that, in response to light, phosphorylates and activates AlgB. Indeed, exposing P. aeruginosa to light represses biofilm formation and virulence gene expression. To our knowledge, P. aeruginosa was not previously known to detect light. The KinB-AlgB-BphP module is present in all Pseudomonads, and we demonstrate that AlgB is the cognate response regulator for BphP in diverse bacterial phyla. We propose that KinB-AlgB-BphP constitutes a “three-component” system and AlgB is the node at which varied sensory information is integrated. This study sets the stage for light-mediated control of P. aeruginosa infectivity.

scholarly journals Conversion of Norepinephrine to 3,4-Dihdroxymandelic Acid in Escherichia coli Requires the QseBC Quorum-Sensing System and the FeaR Transcription Factor

2017 ◽  
Vol 200 (1) ◽  
Author(s):  
Sasikiran Pasupuleti ◽  
Nitesh Sule ◽  
Michael D. Manson ◽  
Arul Jayaraman
Keyword(s):  
Escherichia Coli ◽  
Transcription Factor ◽  
Quorum Sensing ◽  
Aromatic Amines ◽  
Response Regulator ◽  
Content Type ◽  
E Coli ◽  
Expression Of Genes ◽  
K 12 ◽  
Cognate Response Regulator

ABSTRACTThe detection of norepinephrine (NE) as a chemoattractant byEscherichia colistrain K-12 requires the combined action of the TynA monoamine oxidase and the FeaB aromatic aldehyde dehydrogenase. The role of these enzymes is to convert NE into 3,4-dihydroxymandelic acid (DHMA), which is a potent chemoattractant sensed by the Tsr chemoreceptor. These two enzymes must be induced by prior exposure to NE, and cells that are exposed to NE for the first time initially show minimal chemotaxis toward it. The induction of TynA and FeaB requires the QseC quorum-sensing histidine kinase, and the signaling cascade requires new protein synthesis. Here, we demonstrate that the cognate response regulator for QseC, the transcription factor QseB, is also required for induction. The related quorum-sensing kinase QseE appears not to be part of the signaling pathway, but its cognate response regulator, QseF, which is also a substrate for phosphotransfer from QseC, plays a nonessential role. The promoter of thefeaRgene, which encodes a transcription factor that has been shown to be essential for the expression oftynAandfeaB, has two predicted QseB-binding sites. One of these sites appears to be in an appropriate position to stimulate transcription from the P1promoter of thefeaRgene. This study unites two well-known pathways: one for expression of genes regulated by catecholamines (QseBC) and one for expression of genes required for metabolism of aromatic amines (FeaR, TynA, and FeaB). This cross talk allowsE. colito convert the host-derived and chemotactically inert NE into the potent bacterial chemoattractant DHMA.IMPORTANCEThe chemotaxis ofE. coliK-12 to norepinephrine (NE) requires the conversion of NE to 3,4-dihydroxymandleic acid (DHMA), and DHMA is both an attractant and inducer of virulence gene expression for a pathogenic enterohemorrhagicE. coli(EHEC) strain. The induction of virulence by DHMA and NE requires QseC. The results described here show that the cognate response regulator for QseC, QseB, is also required for conversion of NE into DHMA. Production of DHMA requires induction of a pathway involved in the metabolism of aromatic amines. Thus, the QseBC sensory system provides a direct link between virulence and chemotaxis, suggesting that chemotaxis to host signaling molecules may require that those molecules are first metabolized by bacterial enzymes to generate the actual chemoattractant.

scholarly journals Mycobacterium tuberculosis DosS binds H2S through its Fe3+ heme iron to regulate the Dos dormancy regulon

2021 ◽  
Author(s):  
Ritesh R Sevalkar ◽  
Joel N Glasgow ◽  
Martin Pettinati ◽  
Marcelo A Martin ◽  
Vineel P Reddy ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Response Regulator ◽  
Heme Iron ◽  
Sensor Kinase ◽  
New Paradigm ◽  
Heme Pocket ◽  
Expression Of Genes ◽  
Sensor Kinases ◽  
Dynamics Simulations ◽  
Autokinase Activity

Mycobacterium tuberculosis (Mtb) senses and responds to host-derived gasotransmitters NO and CO via heme-containing sensor kinases DosS and DosT and the response regulator DosR. Hydrogen sulfide (H2S) is an important signaling molecule in mammals, but its role in Mtb physiology is unclear. We have previously shown that exogenous H2S can modulate expression of genes in the Dos dormancy regulon via an unknown mechanism(s). Here, we tested the hypothesis that Mtb senses and responds to H2S via the DosS/T/R system. Using UV-Vis and EPR spectroscopy, we show that H2S binds directly to the ferric (Fe3+) heme of DosS (KD = 5.64 uM) but not the ferrous (Fe2+) form. No interaction with DosT was detected. Thus, the mechanism by which DosS senses H2S is different from that for sensing NO and CO, which bind only the ferrous forms of DosS and DosT. Steered Molecular Dynamics simulations show that H2S, and not the charged HS- species, can enter the DosS heme pocket. We also show that H2S increases DosS autokinase activity and subsequent phosphorylation of DosR, and H2S-mediated increases in Dos regulon gene expression is lost in Mtb lacking DosS. Finally, we demonstrate that physiological levels of H2S in macrophages can induce Dos regulon genes via DosS. Overall, these data reveal a novel mechanism whereby Mtb senses and responds to a third host gasotransmitter, H2S, via DosS-Fe3+. These findings highlight the remarkable plasticity of DosS and establish a new paradigm for how bacteria can sense multiple gasotransmitters through a single heme sensor kinase.

scholarly journals Diversity in Sensing and Signaling of Bacterial Sensor Histidine Kinases

Biomolecules ◽  
2021 ◽  
Vol 11 (10) ◽  
pp. 1524
Author(s):  
Eiji Ishii ◽  
Yoko Eguchi
Keyword(s):  
Drug Targets ◽  
Molecular Mechanisms ◽  
Response Regulator ◽  
Signal Perception ◽  
Expression Of Genes ◽  
Two Component Signal Transduction ◽  
Sense And Respond ◽  
Cognate Response Regulator ◽  
And Control ◽  
Novel Drug

Two-component signal transduction systems (TCSs) are widely conserved in bacteria to respond to and adapt to the changing environment. Since TCSs are also involved in controlling the expression of virulence, biofilm formation, quorum sensing, and antimicrobial resistance in pathogens, they serve as candidates for novel drug targets. TCSs consist of a sensor histidine kinase (HK) and its cognate response regulator (RR). Upon perception of a signal, HKs autophosphorylate their conserved histidine residues, followed by phosphotransfer to their partner RRs. The phosphorylated RRs mostly function as transcriptional regulators and control the expression of genes necessary for stress response. HKs sense their specific signals not only in their extracytoplasmic sensor domain but also in their cytoplasmic and transmembrane domains. The signals are sensed either directly or indirectly via cofactors and accessory proteins. Accumulating evidence shows that a single HK can sense and respond to multiple signals in different domains. The underlying molecular mechanisms of how HK activity is controlled by these signals have been extensively studied both biochemically and structurally. In this article, we introduce the wide diversity of signal perception in different domains of HKs, together with their recently clarified structures and molecular mechanisms.

scholarly journals CorR Regulates Multiple Components of Virulence in Pseudomonas syringae pv. tomato DC3000

2006 ◽  
Vol 19 (7) ◽  
pp. 768-779 ◽  
Author(s):  
Aswathy Sreedharan ◽  
Alejandro Penaloza-Vazquez ◽  
Barbara N. Kunkel ◽  
Carol L. Bender
Keyword(s):  
Pseudomonas Syringae ◽  
Biosynthetic Pathway ◽  
Response Regulator ◽  
Tomato Dc3000 ◽  
Tomato Plants ◽  
Coronafacic Acid ◽  
Multiple Components ◽  
Expression Of Genes ◽  
Genes Encoding ◽  
Polymerase Chain

The phytotoxin coronatine (COR) is produced by various pathovars of Pseudomonas syringae, including P. syringae pv. tomato DC3000, which is pathogenic on crucifers and tomato, and P. syringae pv. glycinea PG4180, a soybean pathogen. The COR molecule contains two distinct components, coronafacic acid (CFA) and coronamic acid (CMA), which are intermediates in the COR biosynthetic pathway. In P. syringae pv. tomato DC3000, it is not clear whether corR, which encodes a response regulator, positively regulates CFA and CMA synthesis as it does in P. syringae pv. glycinea PG4180. In this study, a corR mutant of P. syringae pv. tomato DC3000 was constructed and was shown to be defective in the production of COR, CFA, and CMA. Furthermore, disease severity was greatly reduced in tomato plants inoculated with the corR mutant compared with wild-type P. syringae pv. tomato DC3000. We also showed that a mutation in hrpL, which encodes an alternate RNA polymerase sigma factor (σL) required for the expression of genes encoding components of the type III secretion system, abrogated production of COR in P. syringae pv. tomato DC3000. The presence of a potential hrp box, the recognition site for σL, upstream of corR suggested that corR might be regulated by hrpL. This was confirmed in reverse-transcription polymerase chain reaction experiments showing that the upstream effector gene holPtoAA, which was associated with the hrp box, was cotranscribed with corR. Furthermore, studies also were conducted to investigate whether mutations in corR had effects on the expression of hrpL. The corR mutant of P. syringae pv. tomato DC3000 showed both a reduction and delay in the expression of hrpL and was impaired in its ability to elicit a hypersensitive response on Nicotiana benthamiana. A putative CorR-binding site was identified upstream of hrpL, and gel shift studies confirmed the binding of CorR to this region. These results indicate that corR directly impacts the expression of the hrp regulon in P. syringae.

scholarly journals The Regulator OmpR in Yersinia enterocolitica Participates in Iron Homeostasis by Modulating Fur Level and Affecting the Expression of Genes Involved in Iron Uptake

2021 ◽  
Vol 22 (3) ◽  
pp. 1475
Author(s):  
Karolina Jaworska ◽  
Marta Ludwiczak ◽  
Emilia Murawska ◽  
Adrianna Raczkowska ◽  
Katarzyna Brzostek
Keyword(s):  
Iron Homeostasis ◽  
Response Regulator ◽  
In Silico Analysis ◽  
Cellular Level ◽  
Expression Of Genes ◽  
Negative Effect ◽  
Direct Binding ◽  
Positive Effect ◽  
Silico Analysis ◽  
Repressor Activity

In this study, we found that the loss of OmpR, the response regulator of the two-component EnvZ/OmpR system, increases the cellular level of Fur, the master regulator of iron homeostasis in Y. enterocolitica. Furthermore, we demonstrated that transcription of the fur gene from the YePfur promoter is subject to negative OmpR-dependent regulation. Four putative OmpR-binding sites (OBSs) were indicated by in silico analysis of the fur promoter region, and their removal affected OmpR-dependent fur expression. Moreover, OmpR binds specifically to the predicted OBSs which exhibit a distinct hierarchy of binding affinity. Finally, the data demonstrate that OmpR, by direct binding to the promoters of the fecA, fepA and feoA genes, involved in the iron transport and being under Fur repressor activity, modulates their expression. It seems that the negative effect of OmpR on fecA and fepA transcription is sufficient to counteract the indirect, positive effect of OmpR resulting from decreasing the Fur repressor level. The expression of feoA was positively regulated by OmpR and this mode of action seems to be direct and indirect. Together, the expression of fecA, fepA and feoA in Y. enterocolitica has been proposed to be under a complex mode of regulation involving OmpR and Fur regulators.

scholarly journals Genetic Evidence that the α5 Helix of the Receiver Domain of PhoB Is Involved in Interdomain Interactions

2001 ◽  
Vol 183 (7) ◽  
pp. 2204-2211 ◽  
Author(s):  
Mindy P. Allen ◽  
Kimberly B. Zumbrennen ◽  
William R. McCleary
Keyword(s):  
Response Regulator ◽  
Response Regulators ◽  
Receiver Domain ◽  
Intracellular Signals ◽  
Regulator Protein ◽  
Phosphorylation Cascade ◽  
Α Helix ◽  
Interdomain Interactions ◽  
Response Regulator Protein ◽  
Output Domain

ABSTRACT Two-component signaling proteins are involved in transducing environmental stimuli into intracellular signals. Information is transmitted through a phosphorylation cascade that consists of a histidine protein kinase and a response regulator protein. Generally, response regulators are made up of a receiver domain and an output domain. Phosphorylation of the receiver domain modulates the activity of the output domain. The mechanisms by which receiver domains control the activities of their respective output domains are unknown. To address this question for the PhoB protein from Escherichia coli, we have employed two separate genetic approaches, deletion analysis and domain swapping. In-frame deletions were generated within the phoB gene, and the phenotypes of the mutants were analyzed. The output domain, by itself, retained significant ability to activate transcription of the phoA gene. However, another deletion mutant that contained the C-terminal α-helix of the receiver domain (α5) in addition to the entire output domain was unable to activate transcription of phoA. This result suggests that the α5 helix of the receiver domain interacts with and inhibits the output domain. We also constructed two chimeric proteins that join various parts of the chemotaxis response regulator, CheY, to PhoB. A chimera that joins the N-terminal ∼85% of CheY's receiver domain to the β5-α5 loop of PhoB's receiver domain displayed phosphorylation-dependent activity. The results from both sets of experiments suggest that the regulation of PhoB involves the phosphorylation-mediated modulation of inhibitory contacts between the α5 helix of its unphosphorylated receiver domain and its output domain.

scholarly journals Regulation of the Min Cell Division Inhibition Complex by the Rcs Phosphorelay in Proteus mirabilis

2015 ◽  
Vol 197 (15) ◽  
pp. 2499-2507 ◽  
Author(s):  
Kristen E. Howery ◽  
Katy M. Clemmer ◽  
Emrah Şimşek ◽  
Minsu Kim ◽  
Philip N. Rather
Keyword(s):  
Cell Division ◽  
Cell Differentiation ◽  
Proteus Mirabilis ◽  
Cell Elongation ◽  
Response Regulator ◽  
Swarmer Cell ◽  
Content Type ◽  
Expression Of Genes ◽  
Rapid Amplification

ABSTRACTA key regulator of swarming inProteus mirabilisis the Rcs phosphorelay, which repressesflhDC, encoding the master flagellar regulator FlhD4C2. Mutants inrcsB, the response regulator in the Rcs phosphorelay, hyperswarm on solid agar and differentiate into swarmer cells in liquid, demonstrating that this system also influences the expression of genes central to differentiation. To gain a further understanding of RcsB-regulated genes involved in swarmer cell differentiation, transcriptome sequencing (RNA-Seq) was used to examine the RcsB regulon. Among the 133 genes identified,minCandminD, encoding cell division inhibitors, were identified as RcsB-activated genes. A third gene,minE, was shown to be part of an operon withminCD. To examineminCDEregulation, theminpromoter was identified by 5′ rapid amplification of cDNA ends (5′-RACE), and both transcriptionallacZfusions and quantitative real-time reverse transcriptase (qRT) PCR were used to confirm that theminCDEoperon was RcsB activated. Purified RcsB was capable of directly binding theminCpromoter region. To determine the role of RcsB-mediated activation ofminCDEin swarmer cell differentiation, a polarminCmutation was constructed. This mutant formed minicells during growth in liquid, produced shortened swarmer cells during differentiation, and exhibited decreased swarming motility.IMPORTANCEThis work describes the regulation and role of the MinCDE cell division system inP. mirabilisswarming and swarmer cell elongation. Prior to this study, the mechanisms that inhibit cell division and allow swarmer cell elongation were unknown. In addition, this work outlines for the first time the RcsB regulon inP. mirabilis. Taken together, the data presented in this study begin to address howP. mirabiliselongates upon contact with a solid surface.

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