ArticleProceedings of the National Academy of Sciences of the United States of America2024
Fluorescent proteins generate a genetic color polymorphism and counteract oxidative stress in intertidal sea anemones.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 9 citations in OpenAlex.
- UV-Induced Fluorescence in the Balance: Mate Choice and Predation Risk in the Female Ornamented Jumping Spiders.Integrative zoology · 2026Article
- The chromosomal genome sequence of the giant green anemone,Wellcome open research · 2026Article
- Anthozoan Chemical Defenses: Integrating Compounds, Enzymatic Activities, and Omics-Based Discoveries.International journal of molecular sciences · 2025Review
- Regulation of Green Fluorescent Proteins by Sea Anemones (Anthopleura spp.) in Response to Light.Integrative and comparative biology · 2024Article
- The function and consequences of fluorescence in tetrapods.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
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Abstract
Fluorescent proteins (FPs) are ubiquitous tools in research, yet their endogenous functions in nature are poorly understood. In this work, we describe a combination of functions for FPs in a clade of intertidal sea anemones whose FPs control a genetic color polymorphism together with the ability to combat oxidative stress. Focusing on the underlying genetics of a fluorescent green "Neon" color morph, we show that allelic differences in a single FP gene generate its strong and vibrant color, by increasing both molecular brightness and FP gene expression level. Natural variation in FP sequences also produces differences in antioxidant capacity. We demonstrate that these FPs are strong antioxidants that can protect live cells against oxidative stress. Finally, based on structural modeling of the responsible amino acids, we propose a model for FP antioxidant function that is driven by molecular surface charge. Together, our findings shed light on the multifaceted functions that can co-occur within a single FP and provide a framework for studying the evolution of fluorescence as it balances spectral and physiological functions in nature.
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Registered trials
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