scholarly journals Unraveling the role of the CbrA histidine kinase in the signal transduction of the CbrAB two-component system in Pseudomonas putida

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Elizabet Monteagudo-Cascales ◽  
Sofía M. García-Mauriño ◽  
Eduardo Santero ◽  
Inés Canosa
Keyword(s):  
Signal Transduction ◽  
Pseudomonas Putida ◽  
Histidine Kinase ◽  
Two Component System ◽  
Component System ◽  
Two Component

scholarly journals Site-Directed Mutagenesis Identifies a Molecular Switch Involved in Copper Sensing by the Histidine Kinase CinS in Pseudomonas putida KT2440

2009 ◽  
Vol 191 (16) ◽  
pp. 5304-5311 ◽  
Author(s):  
Davide Quaranta ◽  
Megan M. McEvoy ◽  
Christopher Rensing
Keyword(s):  
Pseudomonas Putida ◽  
Histidine Kinase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Copper Binding ◽  
Wild Type ◽  
Two Component System ◽  
Pseudomonas Putida Kt2440 ◽  
Component System ◽  
Two Component

ABSTRACT In the presence of copper, Pseudomonas putida activates transcription of cinAQ via the two-component system CinS-CinR. The CinS-CinR TCS was responsive to 0.5 μM copper and was specifically activated only by copper and silver. Modeling studies of CinS identified a potential copper binding site containing H37 and H147. CinS mutants with H37R and H147R mutations had an almost 10-fold reduced copper-dependent induction of cinAQ compared to the wild type.

scholarly journals Diversity of two-component systems: insights into the signal transduction mechanism by the Staphylococcus aureus two-component system GraSR

F1000Research ◽  
2014 ◽  
Vol 3 ◽  
pp. 252 ◽  
Author(s):  
Uzma Muzamal ◽  
Daniel Gomez ◽  
Fenika Kapadia ◽  
Dasantila Golemi-Kotra
Keyword(s):  
Signal Transduction ◽  
Staphylococcus Aureus ◽  
Abc Transporter ◽  
Histidine Kinase ◽  
Response Regulator ◽  
Two Component System ◽  
Component System ◽  
Transduction Mechanism ◽  
Two Component ◽  
Auxiliary Protein

The response to cationic antimicrobial peptides (CAMPs) in Staphylococcus aureus relies on a two-component system (TCS), GraSR, an auxiliary protein GraX and an ATP-binding cassette (ABC) transporter, VraF/G. To understand the signal transduction mechanism by GraSR, we investigated the kinase activity of the cytoplasmic domain of histidine kinase GraS and the interaction with its cognate response regulator GraR. We also investigated interactions among the auxiliary protein GraX, GraS/R and the ATPase protein of the ABC transporter, VraF. We found that GraS lacks autophosphorylation activity, unlike a similar histidine kinase, BceS, of Bacillus subtilis. In addition, the interaction between GraS and GraR is very weak in comparison to the stronger interaction observed between BceS and its conjugated response regulator, BceR, suggesting that CAMP signaling may not flow directly from GraS to GraR. We found that the auxiliary protein GraX interacts with VraF and GraR, and requires the histidine phosphotransfer and dimerization domain of GraS to interact with this protein. Further, VraF requires the GraS region that connects the membrane-bound domain with the cytoplasmic domain of this protein for interaction with GraS. The interactions of GraX with GraS/R and VraF indicate that GraX may serve as a scaffold to bring these proteins in close proximity to GraS, plausibly to facilitate activation of GraS to ultimately transduce the signal to GraR.

scholarly journals The ColRS Two-Component System Regulates Membrane Functions and Protects Pseudomonas putida against Phenol

2006 ◽  
Vol 188 (23) ◽  
pp. 8109-8117 ◽  
Author(s):  
Paula Ann Kivistik ◽  
Marta Putrinš ◽  
Külliki Püvi ◽  
Heili Ilves ◽  
Maia Kivisaar ◽  
...  
Keyword(s):  
Pseudomonas Putida ◽  
Target Genes ◽  
Type I ◽  
Two Component System ◽  
Component System ◽  
Two Component ◽  
Encoding Gene ◽  
Phenol Tolerance

ABSTRACT As reported, the two-component system ColRS is involved in two completely different processes. It facilitates the root colonization ability of Pseudomonas fluorescens and is necessary for the Tn4652 transposition-dependent accumulation of phenol-utilizing mutants in Pseudomonas putida. To determine the role of the ColRS system in P. putida, we searched for target genes of response regulator ColR by use of a promoter library. Promoter screening was performed on phenol plates to mimic the conditions under which the effect of ColR on transposition was detected. The library screen revealed the porin-encoding gene oprQ and the alginate biosynthesis gene algD occurring under negative control of ColR. Binding of ColR to the promoter regions of oprQ and algD in vitro confirmed its direct involvement in regulation of these genes. Additionally, the porin-encoding gene ompA PP0773 and the type I pilus gene csuB were also identified in the promoter screen. However, it turned out that ompA PP0773 and csuB were actually affected by phenol and that the influence of ColR on these promoters was indirect. Namely, our results show that ColR is involved in phenol tolerance of P. putida. Phenol MIC measurement demonstrated that a colR mutant strain did not tolerate elevated phenol concentrations. Our data suggest that increased phenol susceptibility is also the reason for inhibition of transposition of Tn4652 in phenol-starving colR mutant bacteria. Thus, the current study revealed the role of the ColRS two-component system in regulation of membrane functionality, particularly in phenol tolerance of P. putida.

scholarly journals Diversity of two-component systems: insights into the signal transduction mechanism by the Staphylococcus aureus two-component system GraSR

F1000Research ◽  
2014 ◽  
Vol 3 ◽  
pp. 252 ◽  
Author(s):  
Uzma Muzamal ◽  
Daniel Gomez ◽  
Fenika Kapadia ◽  
Dasantila Golemi-Kotra
Keyword(s):  
Signal Transduction ◽  
Staphylococcus Aureus ◽  
Abc Transporter ◽  
Histidine Kinase ◽  
Response Regulator ◽  
Two Component System ◽  
Component System ◽  
Transduction Mechanism ◽  
Two Component ◽  
Auxiliary Protein

The response to cationic antimicrobial peptides (CAMPs) in Staphylococcus aureus relies on a two-component system (TCS), GraSR, an auxiliary protein GraX and an ATP-binding cassette (ABC) transporter, VraF/G. To understand the signal transduction mechanism by GraSR, we investigated the kinase activity of the cytoplasmic domain of histidine kinase GraS and the interaction with its cognate response regulator GraR. We also investigated interactions among the auxiliary protein GraX, GraS/R and the ATPase protein of the ABC transporter, VraF. We found that GraS lacks autophosphorylation activity, unlike a similar histidine kinase, BceS, of Bacillus subtilis. In addition, the interaction between GraS and GraR is very weak in comparison to the stronger interaction observed between BceS and its conjugated response regulator, BceR, suggesting that CAMP signaling may not flow directly from GraS to GraR. We found that the auxiliary protein GraX interacts with VraF and GraR, and requires the histidine phosphotransfer and dimerization domain of GraS to interact with this protein. Further, VraF requires the GraS region that connects the membrane-bound domain with the cytoplasmic domain of this protein for interaction with GraS. The interactions of GraX with GraS/R and VraF indicate that GraX may serve as a scaffold to bring these proteins in close proximity to GraS, plausibly to facilitate activation of GraS to ultimately transduce the signal to GraR.

scholarly journals 1P046 Molecular mechanism of signal transduction of two-component system protein histidine kinase

2005 ◽  
Vol 45 (supplement) ◽  
pp. S43
Author(s):  
S. Yamada ◽  
S. Akiyama ◽  
H. Sugimoto ◽  
H. Kumita ◽  
K. Ito ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Molecular Mechanism ◽  
Histidine Kinase ◽  
Two Component System ◽  
Component System ◽  
Two Component

scholarly journals Extracytoplasmic PAS-Like Domains Are Common in Signal Transduction Proteins

2009 ◽  
Vol 192 (4) ◽  
pp. 1156-1159 ◽  
Author(s):  
Changsoo Chang ◽  
Christine Tesar ◽  
Minyi Gu ◽  
Gyorgy Babnigg ◽  
Andrzej Joachimiak ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Signal Transduction ◽  
Histidine Kinase ◽  
Pas Domain ◽  
Two Component System ◽  
Component System ◽  
Sensor Histidine Kinase ◽  
Two Component ◽  
Sensor Kinases ◽  
Signal Transduction Proteins

ABSTRACT We present the crystal structure of the extracytoplasmic domain of the Bacillus subtilis PhoR sensor histidine kinase, part of a two-component system involved in adaptation to low environmental phosphate concentrations. In addition to the PhoR structure, we predict that the majority of the extracytoplasmic domains of B. subtilis sensor kinases will adopt a fold similar to the ubiquitous PAS domain.

The role of PhoP/PhoQ two component system in regulating stress adaptation in Cronobacter sakazakii

2021 ◽  
pp. 103851
Author(s):  
Yan Ma ◽  
Yingying Zhang ◽  
Ke Chen ◽  
Lingzhu Zhang ◽  
Yibei Zhang ◽  
...  
Keyword(s):  
Stress Adaptation ◽  
Cronobacter Sakazakii ◽  
Two Component System ◽  
Component System ◽  
Two Component

scholarly journals Regulatory Role of the MisR/S Two-Component System in Hemoglobin Utilization in Neisseria meningitidis

2009 ◽  
Vol 78 (3) ◽  
pp. 1109-1122 ◽  
Author(s):  
Shuming Zhao ◽  
Grisselle E. Montanez ◽  
Pradeep Kumar ◽  
Soma Sannigrahi ◽  
Yih-Ling Tzeng
Keyword(s):  
Posttranscriptional Regulation ◽  
Regulatory Mechanisms ◽  
Two Component System ◽  
Gene Encoding ◽  
Positive Role ◽  
Upstream Gene ◽  
Component System ◽  
Two Component ◽  
Major Surface

ABSTRACT Outer membrane iron receptors are some of the major surface entities that are critical for meningococcal pathogenesis. The gene encoding the meningococcal hemoglobin receptor, HmbR, is both independently transcribed and transcriptionally linked to the upstream gene hemO, which encodes a heme oxygenase. The MisR/S two-component system was previously determined to regulate hmbR transcription, and its hemO and hmbR regulatory mechanisms were characterized further here. The expression of hemO and hmbR was downregulated in misR/S mutants under both iron-replete and iron-restricted conditions, and the downregulation could be reversed by complementation. No significant changes in expression of other iron receptors were detected, suggesting that the MisR/S system specifically regulates hmbR. When hemoglobin was the sole iron source, growth defects were detected in the mutants. Primer extension analysis identified a promoter upstream of the hemO-associated Correia element (CE) and another promoter at the proximal end of CE, and processed transcripts previously identified for other cotranscribed CEs were also detected, suggesting that there may be posttranscriptional regulation. MisR directly interacts with sequences upstream of the CE and upstream of the hmbR Fur binding site and thus independently regulates hemO and hmbR. Analysis of transcriptional reporters of hemO and hmbR further demonstrated the positive role of the MisR/S system and showed that the transcription of hmbR initiated from hemO was significantly reduced. A comparison of the effects of the misS mutation under iron-replete and iron-depleted conditions suggested that activation by the MisR/S system and iron-mediated repression by Fur act independently. Thus, the expression of hemO and hmbR is coordinately controlled by multiple independent regulatory mechanisms, including the MisR/S two-component system.

scholarly journals The Staphylococcus aureus KdpDE Two-Component System Couples Extracellular K+Sensing and Agr Signaling to Infection Programming

2011 ◽  
Vol 79 (6) ◽  
pp. 2154-2167 ◽  
Author(s):  
Ting Xue ◽  
Yibo You ◽  
De Hong ◽  
Haipeng Sun ◽  
Baolin Sun
Keyword(s):  
Staphylococcus Aureus ◽  
Uptake System ◽  
Main Function ◽  
Two Component System ◽  
Component System ◽  
Content Type ◽  
Two Component ◽  
Virulence Regulator ◽  
External K

ABSTRACTThe Kdp system is widely distributed among bacteria. InEscherichia coli, the Kdp-ATPase is a high-affinity K+uptake system and its expression is activated by the KdpDE two-component system in response to K+limitation or salt stress. However, information about the role of this system in many bacteria still remains obscure. Here we demonstrate that KdpFABC inStaphylococcus aureusis not a major K+transporter and that the main function of KdpDE is not associated with K+transport but that instead it regulates transcription for a series of virulence factors through sensing external K+concentrations, indicating that this bacterium might modulate its infectious status through sensing specific external K+stimuli in different environments. Our results further reveal thatS. aureusKdpDE is upregulated by the Agr/RNAIII system, which suggests that KdpDE may be an important virulence regulator coordinating the external K+sensing and Agr signaling during pathogenesis in this bacterium.

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