Characterization of a two component system, Bas1213‐1214, important for oxidative stress in Bacillus anthracis

2018 ◽  
Vol 119 (7) ◽  
pp. 5761-5774 ◽  
Author(s):  
Vatika Gupta ◽  
Kanika Jain ◽  
Rajni Garg ◽  
Anshu Malik ◽  
Pooja Gulati ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Bacillus Anthracis ◽  
Two Component System ◽  
Component System ◽  
Two Component

scholarly journals Kinetic Characterization of the WalRKSpn (VicRK) Two-Component System of Streptococcus pneumoniae: Dependence of WalKSpn (VicK) Phosphatase Activity on Its PAS Domain

2010 ◽  
Vol 192 (9) ◽  
pp. 2346-2358 ◽  
Author(s):  
Alina D. Gutu ◽  
Kyle J. Wayne ◽  
Lok-To Sham ◽  
Malcolm E. Winkler
Keyword(s):  
Amino Acids ◽  
Streptococcus Pneumoniae ◽  
Phosphatase Activity ◽  
Pas Domain ◽  
Kinetic Characterization ◽  
Two Component System ◽  
Histidine Kinases ◽  
Component System ◽  
Two Component

ABSTRACT The WalRK two-component system plays important roles in maintaining cell wall homeostasis and responding to antibiotic stress in low-GC Gram-positive bacteria. In the major human pathogen, Streptococcus pneumoniae, phosphorylated WalR Spn (VicR) response regulator positively controls the transcription of genes encoding the essential PcsB division protein and surface virulence factors. WalR Spn is phosphorylated by the WalK Spn (VicK) histidine kinase. Little is known about the signals sensed by WalK histidine kinases. To gain information about WalK Spn signal transduction, we performed a kinetic characterization of the WalRK Spn autophosphorylation, phosphoryltransferase, and phosphatase reactions. We were unable to purify soluble full-length WalK Spn . Consequently, these analyses were performed using two truncated versions of WalK Spn lacking its single transmembrane domain. The longer version (Δ35 amino acids) contained most of the HAMP domain and the PAS, DHp, and CA domains, whereas the shorter version (Δ195 amino acids) contained only the DHp and CA domains. The autophosphorylation kinetic parameters of Δ35 and Δ195 WalK Spn were similar [Km (ATP) ≈ 37 μM; k cat ≈ 0.10 min−1] and typical of those of other histidine kinases. The catalytic efficiency of the two versions of WalK Spn ∼P were also similar in the phosphoryltransfer reaction to full-length WalR Spn . In contrast, absence of the HAMP-PAS domains significantly diminished the phosphatase activity of WalK Spn for WalR Spn ∼P. Deletion and point mutations confirmed that optimal WalK Spn phosphatase activity depended on the PAS domain as well as residues in the DHp domain. In addition, these WalK Spn DHp domain and ΔPAS mutations led to attenuation of virulence in a murine pneumonia model.

scholarly journals Two-Component System Cross-Regulation Integrates Bacillus anthracis Response to Heme and Cell Envelope Stress

2014 ◽  
Vol 10 (3) ◽  
pp. e1004044 ◽  
Author(s):  
Laura A. Mike ◽  
Jacob E. Choby ◽  
Paul R. Brinkman ◽  
Lorenzo Q. Olive ◽  
Brendan F. Dutter ◽  
...  
Keyword(s):  
Bacillus Anthracis ◽  
Cell Envelope ◽  
Two Component System ◽  
Component System ◽  
Envelope Stress ◽  
Two Component

Characterization of a two-component system, devR-devS, of Mycobacterium tuberculosis

2000 ◽  
Vol 80 (3) ◽  
pp. 141-159 ◽  
Author(s):  
N. Dasgupta ◽  
V. Kapur ◽  
K.K. Singh ◽  
T.K. Das ◽  
S. Sachdeva ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Two Component System ◽  
Component System ◽  
Two Component

Characterization of a Novel Two-Component System in Burkholderia cenocepacia

2014 ◽  
Vol 70 (4) ◽  
pp. 556-561 ◽  
Author(s):  
Callie R. Merry ◽  
Michael Perkins ◽  
Lin Mu ◽  
Bridget K. Peterson ◽  
Rebecca W. Knackstedt ◽  
...  
Keyword(s):  
Burkholderia Cenocepacia ◽  
Two Component System ◽  
Component System ◽  
Two Component

Genome-wide characterization of two-component system (TCS) genes in melon (Cucumis melo L.)

2020 ◽  
Vol 151 ◽  
pp. 197-213 ◽  
Author(s):  
Panjing Liu ◽  
Shuoshuo Wang ◽  
Xiangfei Wang ◽  
Xiaoyu Yang ◽  
Qiang Li ◽  
...  
Keyword(s):  
Cucumis Melo ◽  
Two Component System ◽  
Component System ◽  
Genome Wide ◽  
Two Component ◽  
Cucumis Melo L

Identification and Characterization of the Two-Component System HK8700–RR8701 of Kocuria rhizophila DC2201

2019 ◽  
Vol 38 (6) ◽  
pp. 683-692
Author(s):  
Baohua Chen ◽  
Tingting Zou ◽  
Long Zou ◽  
Haiyan Ni ◽  
Yunhong Huang ◽  
...  
Keyword(s):  
Two Component System ◽  
Component System ◽  
Two Component ◽  
Identification And Characterization ◽  
Kocuria Rhizophila

scholarly journals Genetic and Functional Characterization of the Escherichia coli BarA-UvrY Two-Component System: Point Mutations in the HAMP Linker of the BarA Sensor Give a Dominant-Negative Phenotype

2005 ◽  
Vol 187 (21) ◽  
pp. 7317-7324 ◽  
Author(s):  
Henrik Tomenius ◽  
Anna-Karin Pernestig ◽  
Claudia F. Méndez-Catalá ◽  
Dimitris Georgellis ◽  
Staffan Normark ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Functional Characterization ◽  
Point Mutations ◽  
Dominant Negative ◽  
Site Directed Mutagenesis ◽  
Two Component System ◽  
Component System ◽  
Two Component

ABSTRACT The BarA-UvrY two-component system family is strongly associated with virulence but is poorly understood at the molecular level. During our attempts to complement a barA deletion mutant, we consistently generated various mutated BarA proteins. We reasoned that characterization of the mutants would help us to better understand the signal transduction mechanism in tripartite sensors. This was aided by the demonstrated ability to activate the UvrY regulator with acetyl phosphate independently of the BarA sensor. Many of the mutated BarA proteins had poor complementation activity but could counteract the activity of the wild-type sensor in a dominant-negative fashion. These proteins carried point mutations in or near the recently identified HAMP linker, previously implicated in signal transduction between the periplasm and cytoplasm. This created sensor proteins with an impaired kinase activity and a net dephosphorylating activity. Using further site-directed mutagenesis of a HAMP linker-mutated protein, we could demonstrate that the phosphoaccepting aspartate 718 and histidine 861 are crucial for the dephosphorylating activity. Additional analysis of the HAMP linker-mutated BarA sensors demonstrated that a dephosphorylating activity can operate via phosphotransfer within a tripartite sensor dimer in vivo. This also means that a tripartite sensor can be arranged as a dimer even in the dephosphorylating mode.

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