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Natural animal coloration can be determined by a non-fluorescent GFP homolog
Konstantin A Lukyanov*1; AP Savitsky2; YA Labas3; X Zhao4; SA Lukyanov1
(1) Institute of Bioorganic Chemistry RAS, Miklukho-Maklaya 16/10, Moscow 117871, Russia; (2) Institute of Biochemistry RAS, Leninsky pr. 33, 117071 Moscow, Russia; (3) Institute of Ecology and Evolution RAS, Leninsky pr. 33, 117071 Moscow; (4) CLONTECH Laboratories, Inc., 1020 East Meadow Circle, Palo Alto, CA 94303-4230, USA *(firstname.lastname@example.org)
It is generally accepted that the enormous variety of colors and fluorescent hues displayed by living organisms are determined by low-molecular weight pigments or chromoproteins that typically require a prosthetic group. The only known exception to this rule is green fluorescent protein (GFP) from Aequorea victoria. GFP's fluorescence is entirely due to an internal interaction between amino acids within the protein. Here we found a naturally non-fluorescent homolog of GFP to determine strong purple coloration of tentacles in the sea anemone Anemonia sulcata. Under certain conditions, this novel chromoprotein produces a trace amount of red fluorescence (emission lambda max = 595 nm). The fluorescence demonstrates unique behaviour: its intensity slowly increases in the presence of green light but is instantly inhibited by blue light. The quantum yield of fluorescence can be enhanced dramatically by single amino acid replacement, which probably restores the ancestral fluorescent state of the protein. Other fluorescent variants of the novel protein have emission peaks which are red-shifted up to 610 nm. They demonstrate that long-wavelength fluorescence is attainable in fluorescent proteins.
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