Pedigrees of some mutant strains of Escherichia coli K-12

Bachmann, Barbara J.

doi:10.1128/br.36.4.525-557.1972

Cited by 1,338 publications

(76 citation statements)

References 98 publications

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“…Microbiological assays evaluated the impact of the absence of porins in the MIC of metalloantibiotics, using mutant strains devoid of specific porins, as: JF568, a parental strain derived from E. coli K12 and its derived mutants, E. coli JF701 (devoid of OmpC) and E. coli JF703 (devoid of OmpF) [ 102 , 103 ]; the parental strain E. coli W3110 and the mutant strain E. coli W3110 ΔFΔC (devoid of OmpC and OmpF) [ 27 , 104 ]; and E. coli BE BL21(DE3) and E. coli BE BL21(DE3)omp8, derived from the previous one but devoid of the major outer-membrane porins [ 27 ]. Analysing the extensive data reported for several metalloantibiotics by Gameiro et al, Sousa et al, Feio et al, and Fernandes et al, it is possible to observe no significant change of the MIC of each metalloantibiotic when the porins are not expressed (comparing parental and mutant strains), evidencing that these molecules can translocate into the bacterial cells in a porin-independent way [ 30 , 34 , 35 , 51 ].…”

Section: Metalloantibiotic-membrane Interactionsmentioning

confidence: 99%

Fluoroquinolone-Transition Metal Complexes: A Strategy to Overcome Bacterial Resistance

Ferreira

Gameiro

2021

Microorganisms

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Fluoroquinolones (FQs) are antibiotics widely used in the clinical practice due to their large spectrum of action against Gram‑negative and some Gram-positive bacteria. Nevertheless, the misuse and overuse of these antibiotics has triggered the development of bacterial resistance mechanisms. One of the strategies to circumvent this problem is the complexation of FQs with transition metal ions, known as metalloantibiotics, which can promote different activity and enhanced pharmacological behaviour. Here, we discuss the stability of FQ metalloantibiotics and their possible translocation pathways. The main goal of the present review is to frame the present knowledge on the conjunction of biophysical and biological tools that can help to unravel the antibacterial action of FQ metalloantibiotics. An additional goal is to shed light on the studies that must be accomplished to ensure stability and viability of such metalloantibiotics. Potentiometric, spectroscopic, microscopic, microbiological, and computational techniques are surveyed. Stability and partition constants, interaction with membrane porins and elucidation of their role in the influx, determination of the antimicrobial activity against multidrug‑resistant (MDR) clinical isolates, elucidation of the mechanism of action, and toxicity assays are described for FQ metalloantibiotics.

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Section: Metalloantibiotic-membrane Interactionsmentioning

confidence: 99%

Fluoroquinolone-Transition Metal Complexes: A Strategy to Overcome Bacterial Resistance

Ferreira

Gameiro

2021

Microorganisms

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“…The E. coli strains used in this work were wild-type CGSC5073 (Bachmann, 1972), MC1061 (Sambrook et al, 1989), and BL26, a Lac − derivative of BL21 (Studier and Moffat, 1986). Plasmids pJLACZ (Benito et al, 1993), pJVP1LAC (Corchero et al, 1996), and pM275VP1 (Benito et al, 1995) encode a recombinant E. coli ␤-galactosidase and two ␤-galactosidase fusion proteins, respectively.…”

Section: Bacterial Strains and Plasmidsmentioning

confidence: 99%

Optimized release of recombinant proteins by ultrasonication ofE. coli cells

Feliu

Cubarsi

Villaverde

1998

Biotechnol. Bioeng.

106

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The release kinetics of ␤-galactosidase protein have been determined during small-scale ultrasonication of E. coli cells. Among several studied parameters, ionic strength and cell concentration have the least influence on the rate of protein recovery, whereas sample volume and acoustic power dramatically affect the final yield of soluble protein in the cell-free fraction. The analysis of these critical parameters has prompted us to propose a simple model for E. coli disintegration that only involves acoustic power and sample volume, and which allows prediction of optimal sonication times to recover significant amounts of both natural and recombinant proteins in a given set of relevant conditions.

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“…Genetic experiments were carried out in the E. coli in W3110 genetic background strain (Bachmann, 1972). The W3110 mutant derivatives dnaKdnaJ::Kan R and lon::Kan R (Sakr et al, 2010) have been previously described.…”

Section: Bacterial Strains Phages and Culture Conditionsmentioning

confidence: 99%

Bacterial Hsp90 Facilitates the Degradation of Aggregation-Prone Hsp70–Hsp40 Substrates

Fauvet

Finka

Castanié-Cornet

et al. 2021

Front. Mol. Biosci.

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In eukaryotes, the 90-kDa heat shock proteins (Hsp90s) are profusely studied chaperones that, together with 70-kDa heat shock proteins (Hsp70s), control protein homeostasis. In bacteria, however, the function of Hsp90 (HtpG) and its collaboration with Hsp70 (DnaK) remains poorly characterized. To uncover physiological processes that depend on HtpG and DnaK, we performed comparative quantitative proteomic analyses of insoluble and total protein fractions from unstressed wild-type (WT) Escherichia coli and from knockout mutants ΔdnaKdnaJ (ΔKJ), ΔhtpG (ΔG), and ΔdnaKdnaJΔhtpG (ΔKJG). Whereas the ΔG mutant showed no detectable proteomic differences with wild-type, ΔKJ expressed more chaperones, proteases and ribosomes and expressed dramatically less metabolic and respiratory enzymes. Unexpectedly, we found that the triple mutant ΔKJG showed higher levels of metabolic and respiratory enzymes than ΔKJ, suggesting that bacterial Hsp90 mediates the degradation of aggregation-prone Hsp70–Hsp40 substrates. Further in vivo experiments suggest that such Hsp90-mediated degradation possibly occurs through the HslUV protease.

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Pedigrees of some mutant strains of Escherichia coli K-12

Cited by 1,338 publications

References 98 publications

Fluoroquinolone-Transition Metal Complexes: A Strategy to Overcome Bacterial Resistance

Fluoroquinolone-Transition Metal Complexes: A Strategy to Overcome Bacterial Resistance

Optimized release of recombinant proteins by ultrasonication ofE. coli cells

Bacterial Hsp90 Facilitates the Degradation of Aggregation-Prone Hsp70–Hsp40 Substrates

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