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Updated: Aug 15, 2026

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis
Published on: July 6, 2021
Optimization of DsRed production in Escherichia coli: effect of ribosome binding site sequestration on translation
Brian F Pfleger1, Nicolas J Fawzi, Jay D Keasling
1Department of Chemical Engineering, University of California Berkeley, California, USA.
Abstract:
DsRed-Express, a popular reporter protein, cannot be expressed in Escherichia coli using a consensus ribosome binding site (RBS) potentially due to basepairing in the RBS that inhibits translation initiation. Saturation mutagenesis was used to probe for a gene sequence that minimized basepairing in the RBS while maintaining the same spectral properties and maturation characteristics as DsRed-Express. The new DsRed, designated here as RFP(EC) for E. coli optimized red fluorescent protein, fluoresces 2.5 times greater than DsRed-Express when expressed from the same vector.
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