Chemical Structure of the Hexapeptide Chromophore of the Aequorea Green-Fluorescent Protein

Chris W. Cody; Douglas C. Prasher; William M. Westler; Franklyn G. Prendergast; William W. Ward

doi:10.1021/bi00056a003

Chemical Structure of the Hexapeptide Chromophore of the Aequorea Green-Fluorescent Protein

Chris W. Cody, Douglas C. Prasher, William M. Westler, Franklyn G. Prendergast, William W. Ward

Pharmacology

Research output: Contribution to journal › Article › peer-review

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Abstract

The green-fluorescent proteins (GFP) are a unique class of proteins involved in bioluminescence of many cnidaria. The GFPs serve as energy-transfer acceptors, receiving energy from either a luciferaseoxyluciferin complex or a Ca²⁺-activated photoprotein, depending on the organism. Upon mechanical stimulation of the organism, GFP emits green light spectrally identical to its fluorescence emission. These highly fluorescent proteins are unique due to the nature of the covalently attached chromophore, which is composed of modified amino acid residues within the polypeptide. This report describes the characterization of the Aequorea victoria GFP chromophore which is released as a hexapeptide upon digestion of the protein with papain. The chromophore is formed upon cyclization of the residues Ser-dehydroTyr-Gly within the polypeptide. The chromophore structure proposed here differs from that described by Shimomura [(1979) FEBS Lett. 104, 220] in a number of ways.

Original language	English (US)
Pages (from-to)	1212-1218
Number of pages	7
Journal	Biochemistry
Volume	32
Issue number	5
DOIs	https://doi.org/10.1021/bi00056a003
State	Published - 1993

ASJC Scopus subject areas

Biochemistry

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10.1021/bi00056a003

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title = "Chemical Structure of the Hexapeptide Chromophore of the Aequorea Green-Fluorescent Protein",

abstract = "The green-fluorescent proteins (GFP) are a unique class of proteins involved in bioluminescence of many cnidaria. The GFPs serve as energy-transfer acceptors, receiving energy from either a luciferaseoxyluciferin complex or a Ca2+-activated photoprotein, depending on the organism. Upon mechanical stimulation of the organism, GFP emits green light spectrally identical to its fluorescence emission. These highly fluorescent proteins are unique due to the nature of the covalently attached chromophore, which is composed of modified amino acid residues within the polypeptide. This report describes the characterization of the Aequorea victoria GFP chromophore which is released as a hexapeptide upon digestion of the protein with papain. The chromophore is formed upon cyclization of the residues Ser-dehydroTyr-Gly within the polypeptide. The chromophore structure proposed here differs from that described by Shimomura [(1979) FEBS Lett. 104, 220] in a number of ways.",

author = "Cody, {Chris W.} and Prasher, {Douglas C.} and Westler, {William M.} and Prendergast, {Franklyn G.} and Ward, {William W.}",

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T1 - Chemical Structure of the Hexapeptide Chromophore of the Aequorea Green-Fluorescent Protein

AU - Cody, Chris W.

AU - Prasher, Douglas C.

AU - Westler, William M.

AU - Prendergast, Franklyn G.

AU - Ward, William W.

PY - 1993

Y1 - 1993

N2 - The green-fluorescent proteins (GFP) are a unique class of proteins involved in bioluminescence of many cnidaria. The GFPs serve as energy-transfer acceptors, receiving energy from either a luciferaseoxyluciferin complex or a Ca2+-activated photoprotein, depending on the organism. Upon mechanical stimulation of the organism, GFP emits green light spectrally identical to its fluorescence emission. These highly fluorescent proteins are unique due to the nature of the covalently attached chromophore, which is composed of modified amino acid residues within the polypeptide. This report describes the characterization of the Aequorea victoria GFP chromophore which is released as a hexapeptide upon digestion of the protein with papain. The chromophore is formed upon cyclization of the residues Ser-dehydroTyr-Gly within the polypeptide. The chromophore structure proposed here differs from that described by Shimomura [(1979) FEBS Lett. 104, 220] in a number of ways.

AB - The green-fluorescent proteins (GFP) are a unique class of proteins involved in bioluminescence of many cnidaria. The GFPs serve as energy-transfer acceptors, receiving energy from either a luciferaseoxyluciferin complex or a Ca2+-activated photoprotein, depending on the organism. Upon mechanical stimulation of the organism, GFP emits green light spectrally identical to its fluorescence emission. These highly fluorescent proteins are unique due to the nature of the covalently attached chromophore, which is composed of modified amino acid residues within the polypeptide. This report describes the characterization of the Aequorea victoria GFP chromophore which is released as a hexapeptide upon digestion of the protein with papain. The chromophore is formed upon cyclization of the residues Ser-dehydroTyr-Gly within the polypeptide. The chromophore structure proposed here differs from that described by Shimomura [(1979) FEBS Lett. 104, 220] in a number of ways.

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Chemical Structure of the Hexapeptide Chromophore of the Aequorea Green-Fluorescent Protein

Abstract

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