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Cyan fluorescent proteins derived from mNeonGreen

Authors :
Landon Zarowny
Damien Clavel
Ryan Johannson
Kévin Duarte
Hadrien Depernet
Jérôme Dupuy
Heather Baker
Alex Brown
Antoine Royant
Robert E Campbell
University of Alberta
Institut de biologie structurale (IBS - UMR 5075)
Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG)
Direction de Recherche Fondamentale (CEA) (DRF (CEA))
Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA))
Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)
European Synchroton Radiation Facility [Grenoble] (ESRF)
The University of Tokyo (UTokyo)
the Canadian Institutes of Health Research (CIHR) (FS-154310 to R.E.C.)
the Natural Sciences and Engineering Research Council of Canada (NSERC) (RGPIN 2018-04364 to R.E.C. and RGPIN 2020-04347
the National Institutes of Health (NIH R01GM109984 to Nathan Shaner (UC San Diego)
ANR-17-CE11-0013,BANDIT,d'une Nox bactérienne à la conception d'outil de criblage(2017)
Source :
Protein Engineering, Design and Selection, Protein Engineering, Design and Selection, 2022, 35, pp.1-13. ⟨10.1093/protein/gzac004⟩
Publication Year :
2022
Publisher :
Oxford University Press (OUP), 2022.

Abstract

mNeonGreen, an engineered green fluorescent protein (GFP) derived from lancelet, is one of the most brightly fluorescent homologs of Aequorea victoria jellyfish GFP (avGFP) yet reported. In this work, we investigated whether this bright fluorescence might be retained in homologs of mNeonGreen with modified chromophore structures and altered fluorescent hues. We found mNeonGreen to be generally less tolerant than avGFP to chromophore modification by substitution of the key chromophore-forming tyrosine residue with other aromatic amino acids. However, we were ultimately successful in creating a variant, designated as NeonCyan1, with a tryptophan-derived cyan fluorescent protein (CFP)-type chromophore, and two additional mutants with distinct spectral hues. Structural, computational, and photophysical characterization of NeonCyan1 and its variants provided insight into the factors that control the fluorescence emission color. Though not recommended as replacements for contemporary CFP variants, we demonstrate that NeonCyan1 variants are potentially suitable for live cell imaging applications.

Details

ISSN :
17410134 and 17410126
Volume :
35
Database :
OpenAIRE
Journal :
Protein Engineering, Design and Selection
Accession number :
edsair.doi.dedup.....60f354f7dbaa7a648e54de76bde2f5df