scholarly journals Antagonistic Effect of Nickel on the Fermentative Growth of Escherichia coli K-12 and Comparison of Nickel and Cobalt Toxicity on the Aerobic and Anaerobic Growth

1994 ◽  
Vol 102 ◽  
pp. 297 ◽  
Author(s):  
Long-Fei Wu ◽  
Clarisse Navarro ◽  
Karinne de Pina ◽  
Martine Quenard ◽  
Marie-Andree Mandrand
Keyword(s):  
Escherichia Coli ◽  
Antagonistic Effect ◽  
Anaerobic Growth ◽  
Cobalt Toxicity ◽  
Fermentative Growth ◽  
K 12 ◽  
Aerobic And Anaerobic Growth ◽  
Aerobic And Anaerobic

Fumarate dependent protein composition under aerobic and anaerobic growth conditions in Escherichia coli

2020 ◽  
Vol 212 ◽  
pp. 103583 ◽  
Author(s):  
Kristin Surmann ◽  
Marius Stopp ◽  
Sebastian Wörner ◽  
Vishnu M. Dhople ◽  
Uwe Völker ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Composition ◽  
Growth Conditions ◽  
Anaerobic Growth ◽  
Dependent Protein ◽  
Aerobic And Anaerobic Growth ◽  
Aerobic And Anaerobic

scholarly journals Effect of Intracellular Expression of Antimicrobial Peptide LL-37 on Growth of Escherichia coli Strain TOP10 under Aerobic and Anaerobic Conditions

2013 ◽  
Vol 57 (10) ◽  
pp. 4707-4716 ◽  
Author(s):  
Wei Liu ◽  
Shi Lei Dong ◽  
Fei Xu ◽  
Xue Qin Wang ◽  
T. Ryan Withers ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Growth Conditions ◽  
Anaerobic Growth ◽  
Anaerobic Conditions ◽  
Content Type ◽  
E Coli ◽  
Intracellular Expression ◽  
Aerobic And Anaerobic Growth ◽  
Aerobic And Anaerobic ◽  
Aerobic And Anaerobic Conditions

ABSTRACTAntimicrobial peptides (AMPs) can cause lysis of target bacteria by directly inserting themselves into the lipid bilayer. This killing mechanism confounds the identification of the intracellular targets of AMPs. To circumvent this, we used a shuttle vector containing the inducible expression of a human cathelicidin-related AMP, LL-37, to examine its effect onEscherichia coliTOP10 under aerobic and anaerobic growth conditions. Induction of LL-37 caused growth inhibition and alteration in cell morphology to a filamentous phenotype. Further examination of theE. colicell division protein FtsZ revealed that LL-37 did not interact with FtsZ. Moreover, intracellular expression of LL-37 results in the enhanced production of reactive oxygen species (ROS), causing lethal membrane depolarization under aerobic conditions. Additionally, the membrane permeability was increased after intracellular expression of LL37 under both aerobic and anaerobic conditions. Transcriptomic analysis revealed that intracellular LL-37 mainly affected the expression of genes related to energy production and carbohydrate metabolism. More specifically, genes related to oxidative phosphorylation under both aerobic and anaerobic growth conditions were affected. Collectively, our current study demonstrates that intracellular expression of LL-37 inE. colican inhibit growth under aerobic and anaerobic conditions. While we confirmed that the generation of ROS is a bactericidal mechanism for LL-37 under aerobic growth conditions, we also found that the intracellular accumulation of cationic LL-37 influences the redox and ion status of the cells under both growth conditions. These data suggest that there is a new AMP-mediated bacterial killing mechanism that targets energy metabolism.

Differential effect of YidC depletion on the membrane proteome of Escherichia coli under aerobic and anaerobic growth conditions

PROTEOMICS ◽  
2010 ◽  
Vol 10 (18) ◽  
pp. 3235-3247 ◽  
Author(s):  
Claire E. Price ◽  
Andreas Otto ◽  
Fabrizia Fusetti ◽  
Dörte Becher ◽  
Michael Hecker ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Differential Effect ◽  
Growth Conditions ◽  
Anaerobic Growth ◽  
Membrane Proteome ◽  
Aerobic And Anaerobic Growth ◽  
Aerobic And Anaerobic

scholarly journals Regulation of Aerobic and Anaerobic d-Malate Metabolism of Escherichia coli by the LysR-Type Regulator DmlR (YeaT)

2010 ◽  
Vol 192 (10) ◽  
pp. 2503-2511 ◽  
Author(s):  
Hanna Lukas ◽  
Julia Reimann ◽  
Ok Bin Kim ◽  
Jan Grimpo ◽  
Gottfried Unden
Keyword(s):  
Escherichia Coli ◽  
Malate Dehydrogenase ◽  
Major Effect ◽  
Anaerobic Growth ◽  
Two Component System ◽  
E Coli ◽  
High Level ◽  
K 12 ◽  
Aerobic And Anaerobic ◽  
Malate Metabolism

ABSTRACT Escherichia coli K-12 is able to grow under aerobic conditions on d-malate using DctA for d-malate uptake and the d-malate dehydrogenase DmlA (formerly YeaU) for converting d-malate to pyruvate. Induction of dmlA encoding DmlA required an intact dmlR (formerly yeaT) gene, which encodes DmlR, a LysR-type transcriptional regulator. Induction of dmlA by DmlR required the presence of d-malate or l- or meso-tartrate, but only d-malate supported aerobic growth. The regulator of general C4-dicarboxylate metabolism (DcuS-DcuR two-component system) had some effect on dmlA expression. The anaerobic l-tartrate regulator TtdR or the oxygen sensors ArcB-ArcA and FNR did not have a major effect on dmlA expression. DmlR has a high level of sequence identity (49%) with TtdR, the l- and meso-tartrate-specific regulator of l-tartrate fermentation in E. coli. dmlA was also expressed at high levels under anaerobic conditions, and the bacteria had d-malate dehydrogenase activity. These bacteria, however, were not able to grow on d-malate since the anaerobic pathway for d-malate degradation has a predicted yield of ≤0 ATP/mol d-malate. Slow anaerobic growth on d-malate was observed when glycerol was also provided as an electron donor, and d-malate was used in fumarate respiration. The expression of dmlR is subject to negative autoregulation. The network for regulation and coordination of the central and peripheral pathways for C4-dicarboxylate metabolism by the regulators DcuS-DcuR, DmlR, and TtdR is discussed.

scholarly journals Effect of Anaerobic Growth on Quinolone Lethality with Escherichia coli

2006 ◽  
Vol 51 (1) ◽  
pp. 28-34 ◽  
Author(s):  
Muhammad Malik ◽  
Syed Hussain ◽  
Karl Drlica
Keyword(s):  
Escherichia Coli ◽  
Nalidixic Acid ◽  
Sodium Dodecyl ◽  
Anaerobic Growth ◽  
Aerobic Growth ◽  
Anaerobic Conditions ◽  
Dna Complexes ◽  
Chromosome Fragmentation ◽  
Aerobic And Anaerobic Growth ◽  
Aerobic And Anaerobic

ABSTRACT Quinolone activity against Escherichia coli was examined during aerobic growth, aerobic treatment with chloramphenicol, and anaerobic growth. Nalidixic acid, norfloxacin, ciprofloxacin, and PD161144 were lethal for cultures growing aerobically, and the bacteriostatic activity of each quinolone was unaffected by anaerobic growth. However, lethal activity was distinct for each quinolone with cells treated aerobically with chloramphenicol or grown anaerobically. Nalidixic acid failed to kill cells under both conditions; norfloxacin killed cells when they were grown anaerobically but not when they were treated with chloramphenicol; ciprofloxacin killed cells under both conditions but required higher concentrations than those required with cells grown aerobically; and PD161144, a C-8-methoxy fluoroquinolone, was equally lethal under all conditions. Following pretreatment with nalidixic acid, a shift to anaerobic conditions or the addition of chloramphenicol rapidly blocked further cell death. Formation of quinolone-gyrase-DNA complexes, observed as a sodium dodecyl sulfate (SDS)-dependent drop in cell lysate viscosity, occurred during aerobic and anaerobic growth and in the presence and in the absence of chloramphenicol. However, lethal chromosome fragmentation, detected as a drop in viscosity in the absence of SDS, occurred with nalidixic acid treatment only under aerobic conditions in the absence of chloramphenicol. With PD161144, chromosome fragmentation was detected when the cells were grown aerobically and anaerobically and in the presence and in the absence of chloramphenicol. Thus, all quinolones tested appear to form reversible bacteriostatic complexes containing broken DNA during aerobic growth, during anaerobic growth, and when protein synthesis is blocked; however, the ability to fragment chromosomes and to rapidly kill cells under these conditions depends on quinolone structure.

scholarly journals Acid- and Base-Induced Proteins during Aerobic and Anaerobic Growth of Escherichia coli Revealed by Two-Dimensional Gel Electrophoresis

1999 ◽  
Vol 181 (7) ◽  
pp. 2209-2216 ◽  
Author(s):  
Darcy Blankenhorn ◽  
Judith Phillips ◽  
Joan L. Slonczewski
Keyword(s):  
Escherichia Coli ◽  
Gel Electrophoresis ◽  
Low Ph ◽  
Anaerobic Growth ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
High Ph ◽  
Significant Difference ◽  
Aerobic And Anaerobic Growth ◽  
Aerobic And Anaerobic

ABSTRACT Proteins induced by acid or base, during long-term aerobic or anaerobic growth in complex medium, were identified inEscherichia coli. Two-dimensional gel electrophoresis revealed pH-dependent induction of 18 proteins, nine of which were identified by N-terminal sequencing. At pH 9, tryptophan deaminase (TnaA) was induced to a high level, becoming one of the most abundant proteins observed. TnaA may reverse alkalinization by metabolizing amino acids to produce acidic products. Also induced at high pH, but only in anaerobiosis, was glutamate decarboxylase (GadA). Thegad system (GadA/GadBC) neutralizes acidity and enhances survival in extreme acid; its induction during anaerobic growth may help protect alkaline-grown cells from the acidification resulting from anaerobic fermentation. To investigate possible responses to internal acidification, cultures were grown in propionate, a membrane-permeant weak acid which acidifies the cytoplasm. YfiD, a homologue of pyruvate formate lyase, was induced to high levels at pH 4.4 and induced twofold more by propionate at pH 6; both of these conditions cause internal acidification. At neutral or alkaline pH, YfiD was virtually absent. YfiD is therefore a strong candidate for response to internal acidification. Acid or propionate also increased the expression of alkyl hydroperoxide reductase (AhpC) but only during aerobic growth. At neutral or high pH, AhpC showed no significant difference between aerobic and anaerobic growth. The increase of AhpC in acid may help protect the cell from the greater concentrations of oxidizing intermediates at low pH. Isocitrate lyase (AceA) was induced by oxygen across the pH range but showed substantially greater induction in acid or in base than at pH 7. Additional responses observed included the induction of MalE at high pH and induction of several enzymes of sugar metabolism at low pH: the phosphotransferase system components ManX and PtsH and the galactitol fermentation enzyme GatY. Overall, our results indicate complex relationships between pH and oxygen and a novel permeant acid-inducible gene, YfiD.

scholarly journals pH-Dependent Catabolic Protein Expression during Anaerobic Growth of Escherichia coli K-12

2004 ◽  
Vol 186 (1) ◽  
pp. 192-199 ◽  
Author(s):  
Elizabeth Yohannes ◽  
D. Michael Barnhart ◽  
Joan L. Slonczewski
Keyword(s):  
Escherichia Coli ◽  
Ph Regulation ◽  
Metabolic Enzymes ◽  
Anaerobic Growth ◽  
High Ph ◽  
E Coli ◽  
Catabolic Enzymes ◽  
Periplasmic Proteins ◽  
Ph Dependent ◽  
K 12

ABSTRACT During aerobic growth of Escherichia coli, expression of catabolic enzymes and envelope and periplasmic proteins is regulated by pH. Additional modes of pH regulation were revealed under anaerobiosis. E. coli K-12 strain W3110 was cultured anaerobically in broth medium buffered at pH 5.5 or 8.5 for protein identification on proteomic two-dimensional gels. A total of 32 proteins from anaerobic cultures show pH-dependent expression, and only four of these proteins (DsbA, TnaA, GatY, and HdeA) showed pH regulation in aerated cultures. The levels of 19 proteins were elevated at the high pH; these proteins included metabolic enzymes (DhaKLM, GapA, TnaA, HisC, and HisD), periplasmic proteins (ProX, OppA, DegQ, MalB, and MglB), and stress proteins (DsbA, Tig, and UspA). High-pH induction of the glycolytic enzymes DhaKLM and GapA suggested that there was increased fermentation to acids, which helped neutralize alkalinity. Reporter lac fusion constructs showed base induction of sdaA encoding serine deaminase under anaerobiosis; in addition, the glutamate decarboxylase genes gadA and gadB were induced at the high pH anaerobically but not with aeration. This result is consistent with the hypothesis that there is a connection between the gad system and GabT metabolism of 4-aminobutanoate. On the other hand, 13 other proteins were induced by acid; these proteins included metabolic enzymes (GatY and AckA), periplasmic proteins (TolC, HdeA, and OmpA), and redox enzymes (GuaB, HmpA, and Lpd). The acid induction of NikA (nickel transporter) is of interest because E. coli requires nickel for anaerobic fermentation. The position of the NikA spot coincided with the position of a small unidentified spot whose induction in aerobic cultures was reported previously; thus, NikA appeared to be induced slightly by acid during aeration but showed stronger induction under anaerobic conditions. Overall, anaerobic growth revealed several more pH-regulated proteins; in particular, anaerobiosis enabled induction of several additional catabolic enzymes and sugar transporters at the high pH, at which production of fermentation acids may be advantageous for the cell.

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