The <i>Escherichia coli</i> multiple antibiotic resistance activator protein represses transcription of the <i>lac</i> operon

Lankester, Anna; Ahmed, Shafayeth; Lamberte, Lisa E; Kettles, Rachel A.; Grainger, David C.

doi:10.1042/bst20180498

Cited by 4 publications

(3 citation statements)

References 24 publications

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“…For example, a mutation in the multiple antibiotic resistance (MarR) TRs in Escherichia coli has been shown to lead to the expression of the marRAB operon. Therefore, it promotes the expression of the transcription factor MarA and activation of the acrAB and tolC efflux pump genes, resulting in multi-drug resistance to tetracycline, quinolones, β-lactams, and phenolic compounds ( Pourahmad Jaktaji and Ebadi, 2013 ; Lankester et al, 2019 ). Additionally, the TR EmrR is an inhibitor of efflux pump EmrCAB in Chromobacterium violaceum and the mutation of emrR R92H increases the resistance of C. violaceum to nalidixic acid ( Barroso et al, 2018 ).…”

Section: Introductionmentioning

confidence: 99%

Proteomics Analysis Reveals Bacterial Antibiotics Resistance Mechanism Mediated by ahslyA Against Enoxacin in Aeromonas hydrophila

Zhang

Song

et al. 2021

Front. Microbiol.

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Bacterial antibiotic resistance is a serious global problem; the underlying regulatory mechanisms are largely elusive. The earlier reports states that the vital role of transcriptional regulators (TRs) in bacterial antibiotic resistance. Therefore, we have investigated the role of TRs on enoxacin (ENX) resistance in Aeromonas hydrophila in this study. A label-free quantitative proteomics method was utilized to compare the protein profiles of the ahslyA knockout and wild-type A. hydrophila strains under ENX stress. Bioinformatics analysis showed that the deletion of ahslyA triggers the up-regulated expression of some vital antibiotic resistance proteins in A. hydrophila upon ENX stress and thereby reduce the pressure by preventing the activation of SOS repair system. Moreover, ahslyA directly or indirectly induced at least 11 TRs, which indicates a complicated regulatory network under ENX stress. We also deleted six selected genes in A. hydrophila that altered in proteomics data in order to evaluate their roles in ENX stress. Our results showed that genes such as AHA_0655, narQ, AHA_3721, AHA_2114, and AHA_1239 are regulated by ahslyA and may be involved in ENX resistance. Overall, our data demonstrated the important role of ahslyA in ENX resistance and provided novel insights into the effects of transcriptional regulation on antibiotic resistance in bacteria.

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Section: Introductionmentioning

confidence: 99%

Proteomics Analysis Reveals Bacterial Antibiotics Resistance Mechanism Mediated by ahslyA Against Enoxacin in Aeromonas hydrophila

Zhang

Song

et al. 2021

Front. Microbiol.

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“…So, the organism becomes multiple antibiotic resistant (quinolones, tetracycline, β-lactams, organic solvents, oxidative stress agents and household disinfectants) due to the regulation of the efflux pump and outer membrane porin genes by MarA activations (8,(11)(12)(13). Specifically, MarA is a global transcriptional activator and it has been shown to regulate nearly forty different genes including acrA, acrB and tolC encoding AcrAB-TolC multidrug resistance pump and ompF encoding outer membrane porin OmpF (10,(14)(15)(16). Mar phenotypes were initially detected as being cross-resistant to quinolones, tetracycline, beta-lactams and various phenolic compounds (11).…”

Section: Introductionmentioning

confidence: 99%

Do Norepinephrine and Estradiol Affect the Growth of Escherichia coli and Expressions of Mar Genes?

Gümüş

Yüksek²,

Sefer

et al. 2021

experimed

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Objective: Human hormones have been shown to regulate antibiotic resistance levels, pathogenicity, and growth of bacteria. In our study, we aimed to detect the possible effects of norepinephrine (NE) and estradiol (Est) on growth and expression of chromosomal multiple antibiotic resistance (mar) locus and related genes (ompF, marA, tolC, acrA, marR and acrB) in Escherichia (E) coli SPC105.Material and Method: Serum supplemented SAPI (control) and serum SAPI containing norepinephrine (0.0017 µg/mL, 0.04 µg/ mL, and 100 µg/mL) and estradiol (0.4 ng/mL, 3 ng/mL, 300 ng/mL) was used to grow E. coli SPC105. Growth alterations were determined using the turbidimetric method while the gene expression levels were examined by quantitative polymerase chain reaction (qPCR).Results: It was shown that, NE and Est in all concentrations were shown to affect (reduce/enhance due to incubation periods or hormone concentrations) the growth of E. coli SPC105 apart from the high-level Est concentration. Expression levels of all six target genes were shown to be significantly enhanced in the presence of all concentrations of both NE and Est. Conclusion:Our results constitute new data on the possible influences of these hormones on the growth and expressions of mar operon on transcriptional levels in the E. coli SPC105 strain.

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“…The lacZ gene encodes a β-galactosidase that converts lactose to glucose and galactose; [26] The lacY gene encodes a β-galactoside permease that provides active transport of lactose across the cytoplasmic membrane; and the lacA gene encodes β-galactoside transacetylase, which functions only to transfer acetyl groups on acetyl-coenzyme A to βgalactoside. [27,28] When an inducer (IPTG or lactose) is present, it binds to the repressor protein, which causes a conformational change and inactivates the repressor protein, and prevents it from binding to the operator gene. Therefore, RNA polymerase can transcribe the structural gene (lacZ, lac Y, lac A) into a multiple cis-trans mRNA, and the three enzymes mentioned above are translated.…”

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confidence: 99%

IPTG‐induced high protein expression for whole‐cell biosynthesis of L‐phosphinothricin

Wang

Zhao

et al. 2023

Biotechnology Journal

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BackgroundBiocatalytic production of L‐phosphinothricin (L‐PPT) is currently the most promising method. In this work, we use an Escherichia coli strain coexpressing of D‐amino acid oxidase and catalase (E. coli DAAO‐CAT) to oxidation biocatalytic D‐PPT to PPO, then use the second E. coli strain coexpressing glutamate dehydrogenase and formate dehydrogenase (E. coli GluDH‐FDH) to reduce biocatalytic PPO to L‐PPT.Main Methods and Major ResultsWe compared the effects of different concentrations of IPTG or lactose on protein expression and enzyme activity in 5 L fermenter. The best induction conditions for E. coli DAAO‐CAT were 0.05 mM IPTG, induction for 18 h at 28°C. The specific enzyme activities of DAAO and CAT were 153.20 U g−1 and 896.23 U g−1, respectively. The optimal induction conditions for E. coli GluDH‐FDH were 0.2 mM IPTG, induction for 19 h at 28°C. The specific enzyme activities of GluDH and FDH were 41.72 U g−1 and 109.70 U g−1, respectively. The 200 mM D‐PPT was biocatalyzed by E. coli DAAO‐CAT for 4 h with space‐time yield of 9.0 g·L−1·h−1 and conversion rate of over 99.0%. Then 220 mM PPO was converted to L‐PPT by E. coli GluDH‐FDH for 3 h with space‐time yield of 14.5 g·L−1·h−1 and conversion rate of over 99.0%. To our knowledge, this is the most efficient biocatalytic reaction for L‐PPT production.Conclusions and ImplicationsWe found that IPTG has advantages compared with lactose in the enzyme activity and biomass of E. coli DAAO‐CAT and E. coli GluDH‐FDH, and IPTG is more environmentally friendly. Our data implicated that IPTG can replace lactose in terms of economic feasibility and effectiveness for scaled‐up industrial fermentations.

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The Escherichia coli multiple antibiotic resistance activator protein represses transcription of the lac operon

Cited by 4 publications

References 24 publications

Proteomics Analysis Reveals Bacterial Antibiotics Resistance Mechanism Mediated by ahslyA Against Enoxacin in Aeromonas hydrophila

Proteomics Analysis Reveals Bacterial Antibiotics Resistance Mechanism Mediated by ahslyA Against Enoxacin in Aeromonas hydrophila

Do Norepinephrine and Estradiol Affect the Growth of Escherichia coli and Expressions of Mar Genes?

IPTG‐induced high protein expression for whole‐cell biosynthesis of L‐phosphinothricin

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