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Related Concept Videos

Reporter Genes02:11

Reporter Genes

Reporter genes are a type of protein-coding gene that are often tagged to a gene of interest. Once inside a target cell, reporter genes usually produce visually identifiable characteristics like fluorescence and luminescence when expressed along with the gene of interest. Thus, reporter genes “report” the presence or absence of genes of interest in an organism, determine the gene expression pattern, or track the physical location of a DNA segment or protein in the cell.
Commonly used reporter...

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Application of Genetically Encoded Fluorescent Nitric Oxide (NO&#8226;) Probes, the geNOps, for Real-time Imaging of NO&#8226; Signals in Single Cells
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Engineering a light-controllable fluorescent protein for peroxynitrite detection via genetic code expansion.

Gloricelly M Roman Arocho1, Parthasarathi Das1, Sachin C Tennakoon1

  • 1Department of Chemistry, University of Nebraska - Lincoln Lincoln NE 68588 USA.

RSC Chemical Biology
|June 29, 2026
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Summary

Researchers developed a novel fluorescent protein sensor for detecting peroxynitrite. This new sensor uses a noncanonical amino acid and maintains its light-controllable properties for advanced biological imaging.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Chemical Biology

Background:

  • Peroxynitrite is a reactive nitrogen species implicated in various physiological and pathological processes.
  • Developing selective and sensitive probes for peroxynitrite detection is crucial for understanding its biological roles.
  • Photoconvertible fluorescent proteins offer unique advantages for live-cell imaging due to their controllable fluorescence properties.

Purpose of the Study:

  • To engineer a novel noncanonical amino acid-containing photoconvertible fluorescent protein for selective peroxynitrite detection.
  • To create a peroxynitrite-responsive sensor that retains the photoconversion capability of the parent fluorescent protein.
  • To expand the chemical diversity of light-controllable fluorescent proteins for advanced biological applications.

Main Methods:

  • Site-specific incorporation of the noncanonical amino acid *p*-borono-l-phenylalanine into a circularly permuted mEos2 (cpM2) backbone.
  • Characterization of the resulting protein's spectral properties, photoconversion efficiency, and response to peroxynitrite.
  • Validation of the sensor's performance in vitro and potentially in cellular environments.

Main Results:

  • Successful incorporation of *p*-borono-l-phenylalanine into cpM2 resulted in a novel fluorescent protein.
  • The engineered protein demonstrated specific responsiveness to peroxynitrite, indicated by changes in its fluorescence.
  • The sensor retained its characteristic photoconversion capability, allowing for temporal and spatial control of fluorescence.
  • The sensor expands the toolkit for studying reactive nitrogen species in biological systems.

Conclusions:

  • A noncanonical amino acid-containing photoconvertible fluorescent protein was successfully developed for selective peroxynitrite detection.
  • This engineered sensor offers a valuable tool for real-time monitoring of peroxynitrite dynamics in biological research.
  • The findings contribute to the advancement of chemical biology and fluorescent probe development for imaging reactive species.