scholarly journals Characterization of mutations in the PAS domain of the EvgS sensor kinase selected by laboratory evolution for acid resistance inEscherichia coli

2014 ◽  
Vol 93 (5) ◽  
pp. 911-927 ◽  
Author(s):  
Matthew D. Johnson ◽  
James Bell ◽  
Kim Clarke ◽  
Rachel Chandler ◽  
Prachi Pathak ◽  
...  
Keyword(s):  
Acid Resistance ◽  
Sensor Kinase ◽  
Pas Domain ◽  
Inescherichia Coli ◽  
Laboratory Evolution

scholarly journals Characterization of the PAS domain in the sensor-kinase BvgS: mechanical role in signal transmission

2013 ◽  
Vol 13 (1) ◽  
pp. 172 ◽  
Author(s):  
Elian Dupré ◽  
Alexandre Wohlkonig ◽  
Julien Herrou ◽  
Camille Locht ◽  
Françoise Jacob-Dubuisson ◽  
...  
Keyword(s):  
Signal Transmission ◽  
Sensor Kinase ◽  
Pas Domain

Spectroscopic Characterization of Recombinant Cu,Zn Superoxide Dismutase fromPhotobacterium leiognathiExpressed inEscherichia coli:  Evidence for a Novel Catalytic Copper Binding Site

Biochemistry ◽  
1997 ◽  
Vol 36 (23) ◽  
pp. 7109-7113 ◽  
Author(s):  
Dolly Foti ◽  
Bruno Lo Curto ◽  
Giovanni Cuzzocrea ◽  
M. Elena Stroppolo ◽  
Francesca Polizio ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Binding Site ◽  
Spectroscopic Characterization ◽  
Copper Binding ◽  
Inescherichia Coli

scholarly journals Molecular Cloning and Characterization of the Fusaric Acid-resistance Gene fromPseudomonas cepacia

1991 ◽  
Vol 55 (7) ◽  
pp. 1913-1918
Author(s):  
Ryutaro Utsumi ◽  
Tadashi Yagi ◽  
Satoshi Katayama ◽  
Kiyonori Katsuragi ◽  
Kouji Tachibana ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Resistance Gene ◽  
Fusaric Acid ◽  
Acid Resistance

scholarly journals Cloning and characterization of a haloarchaeal heat shock protein 70 functionally expressed inEscherichia coli

2007 ◽  
Vol 275 (1) ◽  
pp. 168-174 ◽  
Author(s):  
Hao Zhang ◽  
Lu Lin ◽  
Chi Zeng ◽  
Ping Shen ◽  
Yu-Ping Huang
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Inescherichia Coli

scholarly journals Cloning, expression, and antigenic characterization of recombinant protein ofMycoplasma gallisepticum expressed inEscherichia coli

2015 ◽  
Vol 94 (4) ◽  
pp. 621-627 ◽  
Author(s):  
T.S. Rocha ◽  
C. Tramuta ◽  
S. Catania ◽  
A. Matucci ◽  
M.G. Giuffrida ◽  
...  
Keyword(s):  
Recombinant Protein ◽  
Inescherichia Coli ◽  
Antigenic Characterization

Characterization of anAspergillus oryzaeCysteinyl Dipeptidase Expressed inEscherichia coli

2011 ◽  
Vol 75 (1) ◽  
pp. 159-161 ◽  
Author(s):  
Ryota HATTORI ◽  
Mayumi MATSUSHITA-MORITA ◽  
Junichiro MARUI ◽  
Sawaki TADA ◽  
Satoshi SUZUKI ◽  
...  
Keyword(s):  
Inescherichia Coli

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.

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