Fluorescent proteins generate a genetic color polymorphism and counteract oxidative stress in intertidal sea anemones.

Autor:	Clarke DN; Department of Biology, Hopkins Marine Station, Stanford University, Pacific Grove, CA 93950., Rose NH; Department of Biology, Hopkins Marine Station, Stanford University, Pacific Grove, CA 93950., De Meulenaere E; Marine Biology Research Division, Scripps Institution of Oceanography, University of California, San Diego, La Jolla, CA 92037., Rosental B; The Shraga Segal Department of Microbiology, Immunology and Genetics, Faculty of Health Sciences, Center for Regenerative Medicine and Stem Cells, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel., Pearse JS; Department of Ecology and Evolutionary Biology, Joseph M. Long Marine Laboratory, University of California, Santa Cruz, CA 95060., Pearse VB; Department of Biology, Hopkins Marine Station, Stanford University, Pacific Grove, CA 93950.; Department of Ecology and Evolutionary Biology, Joseph M. Long Marine Laboratory, University of California, Santa Cruz, CA 95060., Deheyn DD; Marine Biology Research Division, Scripps Institution of Oceanography, University of California, San Diego, La Jolla, CA 92037.
Jazyk:	angličtina
Zdroj:	Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2024 Mar 12; Vol. 121 (11), pp. e2317017121. Date of Electronic Publication: 2024 Mar 08.
DOI:	10.1073/pnas.2317017121
Abstrakt:	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. Competing Interests: Competing interests statement:The authors declare no competing interest.
Databáze:	MEDLINE
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