scholarly journals Enhancement of the Chaperone Activity of Alkyl Hydroperoxide Reductase C from Pseudomonas aeruginosa PAO1 Resulting from a Point-Specific Mutation Confers Heat Tolerance in Escherichia coli

2016 ◽  
Vol 39 (8) ◽  
pp. 594-602 ◽  
Author(s):  
Jae Taek Lee ◽  
Seung Sik Lee ◽  
Suvendu Mondal ◽  
Bhumi Nath Tripathi ◽  
Siu Kim ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Aeruginosa ◽  
Heat Tolerance ◽  
Chaperone Activity ◽  
Alkyl Hydroperoxide Reductase ◽  
Pseudomonas Aeruginosa Pao1 ◽  
Specific Mutation ◽  
Alkyl Hydroperoxide

scholarly journals Stand-alone ClpG disaggregase confers superior heat tolerance to bacteria

2017 ◽  
Vol 115 (2) ◽  
pp. E273-E282 ◽  
Author(s):  
Changhan Lee ◽  
Kamila B. Franke ◽  
Shady Mansour Kamal ◽  
Hyunhee Kim ◽  
Heinrich Lünsdorf ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Aeruginosa ◽  
Gene Transfer ◽  
Horizontal Gene Transfer ◽  
Atpase Activity ◽  
Stationary Phase ◽  
Virulence Factor ◽  
Heat Tolerance ◽  
Molecular Features ◽  
Partner Proteins

AAA+ disaggregases solubilize aggregated proteins and confer heat tolerance to cells. Their disaggregation activities crucially depend on partner proteins, which target the AAA+ disaggregases to protein aggregates while concurrently stimulating their ATPase activities. Here, we report on two potent ClpG disaggregase homologs acquired through horizontal gene transfer by the species Pseudomonas aeruginosa and subsequently abundant P. aeruginosa clone C. ClpG exhibits high, stand-alone disaggregation potential without involving any partner cooperation. Specific molecular features, including high basal ATPase activity, a unique aggregate binding domain, and almost exclusive expression in stationary phase distinguish ClpG from other AAA+ disaggregases. Consequently, ClpG largely contributes to heat tolerance of P. aeruginosa primarily in stationary phase and boosts heat resistance 100-fold when expressed in Escherichia coli. This qualifies ClpG as a potential persistence and virulence factor in P. aeruginosa.

scholarly journals Catechol biosynthesis from glucose in Escherichia coli anthranilate-overproducer strains by heterologous expression of anthranilate 1,2-dioxygenase from Pseudomonas aeruginosa PAO1

2014 ◽  
Vol 13 (1) ◽  
Author(s):  
Víctor E Balderas-Hernández ◽  
Luis G Treviño-Quintanilla ◽  
Georgina Hernández-Chávez ◽  
Alfredo Martinez ◽  
Francisco Bolívar ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Aeruginosa ◽  
Heterologous Expression ◽  
Pseudomonas Aeruginosa Pao1

Low resolution solution structure of an enzymatic active AhpC 10 :AhpF 2 ensemble of the Escherichia coli Alkyl hydroperoxide Reductase

2016 ◽  
Vol 193 (1) ◽  
pp. 13-22 ◽  
Author(s):  
Neelagandan Kamariah ◽  
Wilson Nartey ◽  
Birgit Eisenhaber ◽  
Frank Eisenhaber ◽  
Gerhard Grüber
Keyword(s):  
Escherichia Coli ◽  
Solution Structure ◽  
Low Resolution ◽  
Alkyl Hydroperoxide Reductase ◽  
Alkyl Hydroperoxide

scholarly journals Role of OxyR as a Peroxide-Sensing Positive Regulator in Streptomyces coelicolor A3(2)

2002 ◽  
Vol 184 (19) ◽  
pp. 5214-5222 ◽  
Author(s):  
Ji-Sook Hahn ◽  
So-Young Oh ◽  
Jung-Hye Roe
Keyword(s):  
Escherichia Coli ◽  
Streptomyces Coelicolor ◽  
Cumene Hydroperoxide ◽  
Exponential Phase ◽  
Alkyl Hydroperoxide Reductase ◽  
Direct Role ◽  
Positive Regulator ◽  
Alkyl Hydroperoxide ◽  
Serovar Typhimurium ◽  
Genes Encoding

ABSTRACT Genes encoding a homolog of Escherichia coli OxyR (oxyR) and an alkyl hydroperoxide reductase system (ahpC and ahpD) have been isolated from Streptomyces coelicolor A3(2). The ahpC and ahpD genes constitute an operon transcribed divergently from the oxyR gene. Expression of both ahpCD and oxyR genes was maximal at early exponential phase and decreased rapidly as cells entered mid-exponential phase. Overproduction of OxyR in Streptomyces lividans conferred resistance against cumene hydroperoxide and H2O2. The oxyR mutant produced fewer ahpCD and oxyR transcripts than the wild type, suggesting that OxyR acts as a positive regulator for their expression. Both oxyR and ahpCD transcripts increased more than fivefold within 10 min of H2O2 treatment and decreased to the normal level in 50 min, with kinetics similar to those of the CatR-mediated induction of the catalase A gene (catA) by H2O2. The oxyR mutant failed to induce oxyR and ahpCD genes in response to H2O2, indicating that OxyR is the modulator for the H2O2-dependent induction of these genes. Purified OxyR protein bound specifically to the intergenic region between ahpC and oxyR, suggesting its direct role in regulating these genes. These results demonstrate that in S. coelicolor OxyR mediates H2O2 induction of its own gene and genes for alkyl hydroperoxide reductase system, but not the catalase gene (catA), unlike in Escherichia coli and Salmonella enterica serovar Typhimurium.

Functional properties and the oligomeric state of alkyl hydroperoxide reductase subunit F (AhpF) in Pseudomonas aeruginosa

PROTOPLASMA ◽  
2020 ◽  
Vol 257 (3) ◽  
pp. 807-817
Author(s):  
Sung Hyun Hong ◽  
Sudhir Singh ◽  
Bhumi Nath Tripathi ◽  
Suvendu Mondal ◽  
Sangmin Lee ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Functional Properties ◽  
Oligomeric State ◽  
Alkyl Hydroperoxide Reductase ◽  
Alkyl Hydroperoxide
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