ArticleNature communications2022
Engineering and exploiting synthetic allostery of NanoLuc luciferase.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 37 citations in OpenAlex.
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- Transient Structural Dynamics of Glycogen Phosphorylase from Nonequilibrium Hydrogen/Deuterium-Exchange Mass Spectrometry.Journal of the American Chemical Society · 2024Article
- Circular permutation at azurin's active site slows down its folding.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023Article
- Illuminating the mechanism and allosteric behavior of NanoLuc luciferase.Nature communications · 2023Article
- Triple Reporter Assay: A Non-Overlapping Luciferase Assay for the Measurement of Complex Macromolecular Regulation in Cancer Cells Using a New Mushroom Luciferase-Luciferin Pair.Sensors (Basel, Switzerland) · 2023Article
- Genetically encoded fluorescent sensors for metals in biology.Current opinion in chemical biology · 2023Review
- Enhancing response of a protein conformational switch by using two disordered ligand binding domains.Frontiers in molecular biosciences · 2023Article
- Bioluminescence Goes Dark: Boosting the Performance of Bioluminescent Sensor Proteins Using Complementation Inhibitors.ACS sensors · 2022Article
- Engineered Amber-Emitting Nano Luciferase and Its Use for Immunobioluminescence ImagingJournal of the American Chemical Society · 2022Article
- A Single-Component Luminescent Biosensor for the SARS-CoV-2 Spike Protein.Journal of the American Chemical Society · 2022Article
- A single-component luminescent biosensor for the SARS-CoV-2 spike protein.bioRxiv : the preprint server for biology · 2022Article
- Engineering protein activity into off-the-shelf DNA devices.Cell reports methods · 2022Article
- Engineering protein and DNA tools for creating DNA-dependent protein switches.Methods in enzymology · 2022Article
Corrections and comments
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Authors and funding
11 authors at 6 institutions in 3 countries.
Funding
Abstract
Allostery enables proteins to interconvert different biochemical signals and form complex metabolic and signaling networks. We hypothesize that circular permutation of proteins increases the probability of functional coupling of new N- and C- termini with the protein's active center through increased local structural disorder. To test this we construct a synthetically allosteric version of circular permutated NanoLuc luciferase that can be activated through ligand-induced intramolecular non-covalent cyclisation. This switch module is tolerant of the structure of binding domains and their ligands, and can be used to create biosensors of proteins and small molecules. The developed biosensors covers a range of emission wavelengths and displays sensitivity as low as 50pM and dynamic range as high as 16-fold and could quantify their cognate ligand in human fluids. We apply hydrogen exchange kinetic mass spectroscopy to analyze time resolved structural changes in the developed biosensors and observe ligand-mediated folding of newly created termini.
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Registered trials
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