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J. Biol. Chem., Vol. 275, Issue 34, 25879-25882, August 25, 2000
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§,
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From the It is generally accepted that the colors
displayed by living organisms are determined by low molecular weight
pigments or chromoproteins that require a prosthetic group. The
exception to this rule is green fluorescent protein (GFP) from
Aequorea victoria that forms a fluorophore by
self-catalyzed protein backbone modification. Here we found a naturally
nonfluorescent 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
Shemiakin and Ovchinnikov Institute of
Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya
16/10, 117871 Moscow, Russia, the ¶ Institute of Ecology and
Evolution and the
Institute of Biochemistry, Russian Academy of
Sciences, Leninsky pr. 33, 117071 Moscow, Russia, and
** CLONTECH Laboratories, Inc., Palo Alto,
California 94303-4230
max = 595 nm). The
fluorescence demonstrates unique behavior: its intensity increases in
the presence of green light but is 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 that are red-shifted up to 610 nm. They demonstrate that long wavelength fluorescence is attainable in GFP-like fluorescent proteins.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF246709
§ These authors contributed equally to this work.
To whom correspondence should be addressed. Tel./Fax:
7-095-330-7056; E-mail: luk@ibch.siobc.ras.ru.
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