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Reporter Genes

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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Updated: Jul 4, 2026

Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence

Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence

Published on: April 27, 2018

Deconstructing green fluorescent protein.

Kevin P Kent¹, William Childs, Steven G Boxer

¹Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-1055, USA.

Journal of the American Chemical Society

|July 4, 2008

Summary

This summary is machine-generated.

Researchers reassembled green fluorescent protein (GFP) from two parts: a large fragment and a synthetic peptide. This novel semisynthetic method allows for studying protein assembly and introducing unnatural amino acids.

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Area of Science:

Biochemistry
Molecular Biology
Biophysics

Background:

Green fluorescent protein (GFP) is a vital tool in molecular biology.
Current methods for GFP modification can be complex.
A split-GFP system offers a potential alternative for protein studies.

Purpose of the Study:

To investigate the feasibility of semisynthetic reassembly of GFP.
To characterize the functional properties of reassembled GFP.
To explore the utility of this method for introducing unnatural amino acids.

Main Methods:

Recombinant expression of a large GFP fragment (GFP 1-10).
Synthesis of a short peptide (synthetic GFP 11) to complete the GFP structure.
Spectroscopic analysis to compare reassembled and whole GFP.

Main Results:

Successfully reassembled functional GFP from two distinct components.
Demonstrated identical absorption and excited-state proton transfer dynamics compared to intact GFP.
Showcased the ability to disassemble and replace the synthetic peptide, altering chromophore absorption.

Conclusions:

Semisynthetic reassembly of GFP is a viable strategy.
This approach provides a versatile platform for studying beta-barrel assembly.
Enables the incorporation of unnatural amino acids into the GFP structure.