scholarly journals Structural and Functional Characterization of Malate Synthase G from Opportunistic Pathogen Pseudomonas aeruginosa

Biochemistry ◽  
2017 ◽  
Vol 56 (41) ◽  
pp. 5539-5549 ◽  
Author(s):  
Alyssa C. McVey ◽  
Prasanthi Medarametla ◽  
Xavier Chee ◽  
Sean Bartlett ◽  
Antti Poso ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Functional Characterization ◽  
Opportunistic Pathogen ◽  
Malate Synthase ◽  
Malate Synthase G

scholarly journals Acquisition of multidrug resistance transposon Tn6061 and IS6100-mediated large chromosomal inversions in Pseudomonas aeruginosa clinical isolates

Microbiology ◽  
2010 ◽  
Vol 156 (5) ◽  
pp. 1448-1458 ◽  
Author(s):  
Sébastien Coyne ◽  
Patrice Courvalin ◽  
Marc Galimand
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Multidrug Resistance ◽  
Opportunistic Pathogen ◽  
Clinical Isolates ◽  
Chromosomal Inversions ◽  
Gene Acquisition ◽  
Drug Classes ◽  
Horizontal Acquisition

Pseudomonas aeruginosa is a major human opportunistic pathogen, especially for patients in intensive care units or with cystic fibrosis. Multidrug resistance is a common feature of this species. In a previous study we detected the ant(4′)-IIb gene in six multiresistant clinical isolates of P. aeruginosa, and determination of the environment of the gene led to characterization of Tn6061. This 26 586 bp element, a member of the Tn3 family of transposons, carried 10 genes conferring resistance to six drug classes. The ant(4′)-IIb sequence was flanked by directly repeated copies of ISCR6 in all but one of the strains studied, consistent with ISCR6-mediated gene acquisition. Tn6061 was chromosomally located in six strains and plasmid-borne in the remaining isolate, suggesting horizontal acquisition. Duplication-insertion of IS6100, that ended Tn6061, was responsible for large chromosomal inversions. Acquisition of Tn6061 and chromosomal inversions are further examples of intricate mechanisms that contribute to the genome plasticity of P. aeruginosa.

scholarly journals Structural and Functional Characterization of Pseudomonas aeruginosa Global Regulator AmpR

2014 ◽  
Vol 196 (22) ◽  
pp. 3890-3902 ◽  
Author(s):  
O. Caille ◽  
D. Zincke ◽  
M. Merighi ◽  
D. Balasubramanian ◽  
H. Kumari ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Functional Characterization ◽  
Global Regulator

scholarly journals Characterization of a Multigene-Encoded Sodium/Hydrogen Antiporter (Sha) from Pseudomonas aeruginosa: Its Involvement in Pathogenesis

2005 ◽  
Vol 187 (15) ◽  
pp. 5242-5248 ◽  
Author(s):  
Saori Kosono ◽  
Koki Haga ◽  
Rui Tomizawa ◽  
Yusuke Kajiyama ◽  
Kazuo Hatano ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Critical Role ◽  
Opportunistic Pathogen ◽  
Growth Defect ◽  
Monovalent Cations ◽  
Sodium Hydrogen ◽  
Tract Infections ◽  
Transport Complex ◽  
Six Genes

ABSTRACT Sha (also known as Mrp/Mnh/Pha) is a Na+/H+ antiporter encoded by a cluster of six or seven genes that probably form a multisubunit transport complex. The Sha system is important for the homeostasis of H+, Na+, and other monovalent cations and plays a critical role in various functions, including alkaliphily, sporulation, and symbiosis. Here, we characterized the sha homologue genes from the opportunistic pathogen Pseudomonas aeruginosa, which exist as a cluster of six genes (PA1054 to PA1059). The gene cluster PA1054 to PA1059, but not the cluster with a deletion of PA1054, complemented a growth defect in the presence of 0.2 M NaCl and a defect in Na+/H+ antiport activity of the Escherichia coli TO114 mutant lacking the three major Na+/H+ antiporters, indicating that genes PA1054 to PA1059 are responsible for Na+/H+ antiport activity. We disrupted PA1054 (a shaA homologue gene) and determined its effect on Na+ tolerance during growth, Na+ efflux, and pathogenicity in mice. Disruption of PA1054 resulted in severe Na+ sensitivity during growth and decreased Na+ efflux activity. In mice, the deletion mutant of PA1054 also exhibited an attenuated virulence in systemic, pulmonary, and urinary tract infections and also a decrease in colonization of the infected organs. From these results, we conclude that the genes PA1054 to PA1059 encode a Na+/H+ antiporter that is largely responsible for Na+ extrusion in P. aeruginosa and has a role in the infection of the pathogen. We propose to designate PA1054 to PA1059 as the sha (sodium hydrogen antiporter) genes, shaABCDEFG.

Functional characterization of two alkane hydroxylases in a versatile Pseudomonas aeruginosa strain NY3

2017 ◽  
Vol 67 (7) ◽  
pp. 459-468 ◽  
Author(s):  
Yan Wang ◽  
Maiqian Nie ◽  
Yi Wan ◽  
Xiaoting Tian ◽  
Hongyun Nie ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Functional Characterization ◽  
Alkane Hydroxylases

scholarly journals Cloning and functional characterization of the Pseudomonas aeruginosa rhlC gene that encodes rhamnosyltransferase 2, an enzyme responsible for di-rhamnolipid biosynthesis

2001 ◽  
Vol 40 (3) ◽  
pp. 708-718 ◽  
Author(s):  
Rahim Rahim ◽  
Urs A. Ochsner ◽  
Clarita Olvera ◽  
Michael Graninger ◽  
Paul Messner ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Functional Characterization

Identification and functional characterization of pfm, a novel gene involved in swimming motility of Pseudomonas aeruginosa

Gene ◽  
2007 ◽  
Vol 401 (1-2) ◽  
pp. 19-27 ◽  
Author(s):  
Fang Bai ◽  
Yingli Li ◽  
Haijing Xu ◽  
Huiming Xia ◽  
Tengfei Yin ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Functional Characterization ◽  
Swimming Motility ◽  
Novel Gene

scholarly journals Characterization of βαβββ Resistance Proteins from Pseudomonas aeruginosa

2014 ◽  
Vol 70 (a1) ◽  
pp. C717-C717
Author(s):  
Allegra Vit ◽  
Monika Popp ◽  
Eyad Kalawy-Fansa ◽  
Shen Yu ◽  
Wulf Blankenfeldt
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Physiological Function ◽  
Functional Characterization ◽  
Conserved Residues ◽  
X Ray ◽  
Resistance Proteins ◽  
X Ray Crystallography ◽  
Phenazine Derivative ◽  
Function Assignment

Pseudomonas aeruginosa is a multiresistant pathogen that can cause infection in immuno-compromized patients, for example in people suffering from cystic fibrosis. [1] It has complex patho-physiology and produces a large number of exoproducts, among which the phenazines are especially prominent. In P. aeruginosa, the blue phenazine derivative pyocyanin plays a crucial role in infection of the host. [2] This phenazine can generate reactive oxygen species and is thought to act as respiratory pigment and as a virulence factor at the same time. P. aeruginosa has to protect itself from its own phenazines because of the antibiotic action of these substances. Inspired by the fact that the phenazine biosynthesis operon of several bacteria contains a phenazine resistance factor of the βαβββ module protein family, we have searched the genome of P. aeruginosa for proteins of this fold. [3] In P. aeruginosa we could identify 22 of these genes, most without previous functional characterization. A structure-based sequence alignment made it possible to assign these proteins to two classes with two subgroups each, based on the conserved residues in the active site. Using X-ray crystallography and biophysical methods, we further demonstrate that several of these proteins indeed bind phenazines and possibly other antibiotics that contain aromatic moieties. Currently, we are working on the structural characterization and physiological function assignment of all of these βαβββ-module-containing proteins. Ultimately, these data may lead to novel anti-infective strategies.

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