TY - JOUR
T1 - Fluorescent proteins generate a genetic color polymorphism and counteract oxidative stress in intertidal sea anemones
AU - Clarke, D. Nathaniel
AU - Rose, Noah H.
AU - De Meulenaere, Evelien
AU - Rosental, Benyamin
AU - Pearse, John S.
AU - Pearse, Vicki Buchsbaum
AU - Deheyn, Dimitri D.
PY - 2024/3/12
Y1 - 2024/3/12
N2 - 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.
AB - 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.
KW - Anthopleura
KW - GFP
KW - antioxidant
KW - biofluorescence
KW - polymorphism
UR - http://www.scopus.com/inward/record.url?scp=85187523244&partnerID=8YFLogxK
U2 - 10.1073/pnas.2317017121
DO - 10.1073/pnas.2317017121
M3 - Article
C2 - 38457522
AN - SCOPUS:85187523244
SN - 0027-8424
VL - 121
SP - e2317017121
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 11
ER -