Bacterial luciferase: Molecular mechanisms and applications

Tinikul, Ruchanok; Chunthaboon, Paweenapon; Phonbuppha, Jittima; Paladkong, Tanakan

doi:10.1016/bs.enz.2020.06.001

Cited by 18 publications

(11 citation statements)

References 98 publications

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“…These nutritional conditions are obviously critical because they contribute to the maintenance of cell viability, required metabolic function, resistance function, and renewal cell functions [3]. They further condition the performance of the biosensors by supplying the energy source (e.g., amino acids and sugars) necessary to sustain the production of bioluminescence [32][33][34][35][36]. This energy demand can be more or less satisfied depending on nutrient bioavailability, cell concentration and the occurrence of nutrient complexation in solution or their adsorption onto abiotic particles [37].…”

Section: Introductionmentioning

confidence: 99%

Exploiting Catabolite Repression and Stringent Response to Control Delay and Multimodality of Bioluminescence Signal by Metal Whole-Cell Biosensors: Interplay between Metal Bioavailability and Nutritional Medium Conditions

et al. 2022

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The time-dependent response of metal-detecting whole-cell luminescent bacterial sensors is impacted by metal speciation/bioavailability in solution. The comprehensive understanding of such connections requires the consideration of the bacterial energy metabolism at stake and the effects of supplied food on cells’ capability to convert bioaccumulated metals into light. Accordingly, we investigated the time response (48 h assay) of PzntA-luxCDABE Escherichia coli Cd biosensors in media differing with respect to sources of amino acids (tryptone or Lysogeny Broth) and carbon (glucose, xylose and mixtures thereof). We show that the resulting coupling between the stringent cell response and glucose/xylose-mediated catabolite repressions lead to well-defined multimodalities and shapes of the bioluminescence signal over time. Based on a recent theory for the time–response of metal-sensing luminescent bacteria, successful theoretical reconstructions of the bioluminescence signals are reported under all Cd concentrations (0–20 nM) and nutritive conditions examined. This analysis leads to the evaluation of time-dependent cell photoactivity and qualitative information on metal speciation/bioavailability in solution. Biosensor performance and the position, shape, number, and magnitude of detected peaks are discussed in relation to the metabolic pathways operative during the successive light emission modes identified here over time. Altogether, the results clarify the contributions of metal/nutrient bio-availabilities and food quality to cell response typology.

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Section: Introductionmentioning

confidence: 99%

Exploiting Catabolite Repression and Stringent Response to Control Delay and Multimodality of Bioluminescence Signal by Metal Whole-Cell Biosensors: Interplay between Metal Bioavailability and Nutritional Medium Conditions

et al. 2022

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“…These chemical reactions ensure bioluminescence in living organisms, which serves various important functions. Bacterial luciferase catalyzes the oxidation of reduced flavin mononucleotides and long chain aliphatic aldehydes accompanied by the generation of blue-greenish light [ 5 ]. This enzymatic reaction is widely used as a reporter system in different fields, including molecular biology [ 6 ], environmental monitoring [ 7 ] and medical diagnostics [ 8 ].…”

Section: Introductionmentioning

confidence: 99%

Bacterial Luciferases from Vibrio harveyi and Photobacterium leiognathi Demonstrate Different Conformational Stability as Detected by Time-Resolved Fluorescence Spectroscopy

Nemtseva

Gulnov

Gerasimova

et al. 2021

IJMS

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Detecting the folding/unfolding pathways of biological macromolecules is one of the urgent problems of molecular biophysics. The unfolding of bacterial luciferase from Vibrio harveyi is well-studied, unlike that of Photobacterium leiognathi, despite the fact that both of them are actively used as a reporter system. The aim of this study was to compare the conformational transitions of these luciferases from two different protein subfamilies during equilibrium unfolding with urea. Intrinsic steady-state and time-resolved fluorescence spectra and circular dichroism spectra were used to determine the stages of the protein unfolding. Molecular dynamics methods were applied to find the differences in the surroundings of tryptophans in both luciferases. We found that the unfolding pathway is the same for the studied luciferases. However, the results obtained indicate more stable tertiary and secondary structures of P. leiognathi luciferase as compared to enzyme from V. harveyi during the last stage of denaturation, including the unfolding of individual subunits. The distinctions in fluorescence of the two proteins are associated with differences in the structure of the C-terminal domain of α-subunits, which causes different quenching of tryptophan emissions. The time-resolved fluorescence technique proved to be a more effective method for studying protein unfolding than steady-state methods.

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“…Though not commonly studied in the context of one- or two-component signaling, SpoIIE is known to de-phosphorylate the sulfate transporter and anti-sigma factor antagonist (STAS) domain containing protein, SpoIIAA, in the process of regulation of a sporulation-specific transcription factor, σ F [93] , [94] , [95] . In addition to these three main groups, we also identified several oxygenases, including bacterial luciferase, ABM monooxygenase, hemeoxygenase and p450 which might be responsible for sensing and degrading respective chemicals such as flavin, antibiotics, and heme [96] , [97] , [98] .…”

Section: Resultsmentioning

confidence: 99%

Photoglobin, a distinct family of non-heme binding globins, defines a potential photosensor in prokaryotic signal transduction systems

Schneider

Tan

et al. 2022

Computational and Structural Biotechnology Journal

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Bacterial luciferase: Molecular mechanisms and applications

Cited by 18 publications

References 98 publications

Exploiting Catabolite Repression and Stringent Response to Control Delay and Multimodality of Bioluminescence Signal by Metal Whole-Cell Biosensors: Interplay between Metal Bioavailability and Nutritional Medium Conditions

Exploiting Catabolite Repression and Stringent Response to Control Delay and Multimodality of Bioluminescence Signal by Metal Whole-Cell Biosensors: Interplay between Metal Bioavailability and Nutritional Medium Conditions

Bacterial Luciferases from Vibrio harveyi and Photobacterium leiognathi Demonstrate Different Conformational Stability as Detected by Time-Resolved Fluorescence Spectroscopy

Photoglobin, a distinct family of non-heme binding globins, defines a potential photosensor in prokaryotic signal transduction systems

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