Bright and photostable yellow fluorescent proteins for extended imaging

Jihwan Lee, Shujuan Lai, Shuyuan Yang, Shiqun Zhao, Francisco A. Blanco, Anne C. Lyons, Raquel Merino-Urteaga, John F. Ahrens, Nathan A. Nguyen, Haixin Liu, Zhuohe Liu, Gerard G. Lambert, Nathan C. Shaner, Liangyi Chen, Kimberley F. Tolias, Jin Zhang, Taekjip Ha and François St-Pierre ()
Additional contact information
Jihwan Lee: Baylor College of Medicine
Shujuan Lai: Baylor College of Medicine
Shuyuan Yang: Rice University
Shiqun Zhao: Peking University
Francisco A. Blanco: Baylor College of Medicine
Anne C. Lyons: University of California San Diego
Raquel Merino-Urteaga: Boston Children’s Hospital
John F. Ahrens: Rice University
Nathan A. Nguyen: Rice University
Haixin Liu: Baylor College of Medicine
Zhuohe Liu: Baylor College of Medicine
Gerard G. Lambert: University of California San Diego School of Medicine
Nathan C. Shaner: University of California San Diego
Liangyi Chen: Peking University
Kimberley F. Tolias: Baylor College of Medicine
Jin Zhang: University of California San Diego
Taekjip Ha: Boston Children’s Hospital
François St-Pierre: Baylor College of Medicine

Nature Communications, 2025, vol. 16, issue 1, 1-16

Abstract: Abstract Fluorescent proteins are indispensable molecular tools for visualizing biological structures and processes, but their limited photostability restricts the duration of dynamic imaging experiments. Yellow fluorescent proteins (YFPs), in particular, photobleach rapidly. Here, we introduce mGold2s and mGold2t, YFPs with up to 25-fold greater photostability than mVenus and mCitrine, two commonly used YFPs, while maintaining comparable brightness. These variants were identified using a high-throughput pooled single-cell platform, simultaneously screening for high brightness and photostability. Compared with our previous benchmark, mGold, the mGold2 variants display a ~4-fold increase in photostability without sacrificing brightness. mGold2s and mGold2t extend imaging durations across diverse modalities, including widefield, total internal reflection fluorescence (TIRF), super-resolution, single-molecule, and laser-scanning confocal microscopy. When incorporated into fluorescence resonance energy transfer (FRET)-based biosensors, the proposed YFPs enable more reliable, prolonged imaging of dynamic cellular processes. Overall, the enhanced photostability of mGold2s and mGold2t enables high-sensitivity imaging of subcellular structures and cellular activity over extended periods, broadening the scope and precision of biological imaging.

Date: 2025
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-025-58223-5 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-58223-5

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-025-58223-5

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().