Engineering a Bright Near-Infrared Fluorescent Protein by Screening a Comprehensive Phenotypic Landscape
Kulhanek, D.; Wei, Q.; Head, J.; Hellinger, J.; Jansen, Z.; Gilmour, A.; Segall-Shapiro, T.; Brodbelt, J. S.; Usama, S. M.; Thyer, R.
Show abstract
Near-infrared fluorescent proteins (niRFPs) are valuable markers for tracking cellular phenomena as they offer greater imaging depth, lower background, and minimal invasiveness relative to other fluorescent probes. The small ultra red fluorescent protein (smURFP) is the brightest niRFP currently reported and has been the subject of several mutagenesis studies to improve its biophysical characteristics. Here, we demonstrate a systematic approach to exploring the mutational landscape of smURFP using a comprehensive deep mutational scanning (DMS) library to identify novel smURFP mutations which confer greater in vivo fluorescence. By observing changes in relative abundance between naive and fluorescence sorted populations, we provide analysis of the enrichment of all possible single-codon substitutions, insertions, and deletions for smURFP. Enriched populations yielded a series of seven single-codon substitutions which confer a three-fold increase in in vivo fluorescence in E. coli when combined. Finally, we assess the potential underlying mechanisms for increased fluorescence by characterizing the biophysical and photophysical properties of the mutant niRFP sequences. We confirm that two of the derived smURFP sequences have a higher molecular brightness than wild type and yield the brightest niRFP reported.
Matching journals
The top 2 journals account for 50% of the predicted probability mass.
Similar papers in this journal
Similar papers in this journal
- Versatile labeling and detection ofendogenous proteins using tag-assistedsplit enzyme complementation 95%
- Improvement of phycocyanobilin synthesis for genetically encoded phytochrome-based optogenetics. 94%
- Development of a new DHFR-based destabilizing domain with enhanced basal turnover and applicability in mammalian systems 94%
Similar papers in this journal
- Decoding mEos4b Day-Long Maturation and Engineering Fast Maturing Variants 95%
- MemPPI platform for measuring and engineering membrane protein-protein interactions in mammalian cells via split nanoluciferase 94%
- Design of a symmetry-broken tetrahedral protein cage by a method of internal steric occlusion 93%
Similar papers in this journal
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.