Primary structure of the Aequorea victoria green-fluorescent protein

Douglas C. Prasher; Virginia K. Eckenrode; William W. Ward; Frank G. Prendergast; Milton J. Cormier

doi:10.1016/0378-1119(92)90691-H

Primary structure of the Aequorea victoria green-fluorescent protein

Douglas C. Prasher, Virginia K. Eckenrode, William W. Ward, Frank G. Prendergast, Milton J. Cormier

Pharmacology

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

1675 Scopus citations

Abstract

Many cnidarians utilize green-fluorescent proteins (GFPs) as energy-transfer acceptors in bioluminescence. GFPs fluoresce in vivo upon receiving energy from either a luciferase-oxyluciferin excited-state complex or a Ca²⁺-activated photoprotein. These highly fluorescent proteins are unique due to the chemical nature of their chromophore, which is comprised of modified amino acid (aa) residues within the polypeptide. This report describes the cloning and sequencing of both cDNA and genomic clones of GFP from the cnidarian, Aequorea victoria. The gfp10 cDNA encodes a 238-aa-residue polypeptide with a calculated M_r of 26888. Comparsion of A. victoria GFP genomic clones shows three different restriction enzyme patterns which suggests that at least three different genes are present in the A. victoria population at Friday Harbor, Washington. The gfp gene encoded by the λGFP2 genomic clone is comprised of at least three exons spread over 2.6 kb. The nucleotide sequences of the cDNA and the gene will aid in the elucidation of structure-function relationships in this unique class of proteins.

Original language	English (US)
Pages (from-to)	229-233
Number of pages	5
Journal	Gene
Volume	111
Issue number	2
DOIs	https://doi.org/10.1016/0378-1119(92)90691-H
State	Published - Feb 15 1992

Keywords

Bioluminescence
Cnidaria
aequorin
chromophore
cloning
energy transfer

ASJC Scopus subject areas

Genetics

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10.1016/0378-1119(92)90691-H

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title = "Primary structure of the Aequorea victoria green-fluorescent protein",

abstract = "Many cnidarians utilize green-fluorescent proteins (GFPs) as energy-transfer acceptors in bioluminescence. GFPs fluoresce in vivo upon receiving energy from either a luciferase-oxyluciferin excited-state complex or a Ca2+-activated photoprotein. These highly fluorescent proteins are unique due to the chemical nature of their chromophore, which is comprised of modified amino acid (aa) residues within the polypeptide. This report describes the cloning and sequencing of both cDNA and genomic clones of GFP from the cnidarian, Aequorea victoria. The gfp10 cDNA encodes a 238-aa-residue polypeptide with a calculated Mr of 26888. Comparsion of A. victoria GFP genomic clones shows three different restriction enzyme patterns which suggests that at least three different genes are present in the A. victoria population at Friday Harbor, Washington. The gfp gene encoded by the λGFP2 genomic clone is comprised of at least three exons spread over 2.6 kb. The nucleotide sequences of the cDNA and the gene will aid in the elucidation of structure-function relationships in this unique class of proteins.",

keywords = "Bioluminescence, Cnidaria, aequorin, chromophore, cloning, energy transfer",

author = "Prasher, {Douglas C.} and Eckenrode, {Virginia K.} and Ward, {William W.} and Prendergast, {Frank G.} and Cormier, {Milton J.}",

note = "Funding Information: We want to extend our thanks to Bonnie Woodward, Darlene Bianca, and Richard McCann for their excellent technical assistance. Supported in part by a Mellon Award from the Woods Hole Oceanographic Institution (27/50.44) and a grant from the American Cancer Society (NP640) to D.C.P. A paper of the journal series New Jersey Agricultural Experiment Station. This work was performed as part of NJAES Project No. 01102. A special thanks goes to Dr. A.O.D. Willows, Director, Friday Harbor Laboratories, fur use of laboratory facilities.",

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doi = "10.1016/0378-1119(92)90691-H",

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AU - Prasher, Douglas C.

AU - Eckenrode, Virginia K.

AU - Ward, William W.

AU - Prendergast, Frank G.

AU - Cormier, Milton J.

N1 - Funding Information: We want to extend our thanks to Bonnie Woodward, Darlene Bianca, and Richard McCann for their excellent technical assistance. Supported in part by a Mellon Award from the Woods Hole Oceanographic Institution (27/50.44) and a grant from the American Cancer Society (NP640) to D.C.P. A paper of the journal series New Jersey Agricultural Experiment Station. This work was performed as part of NJAES Project No. 01102. A special thanks goes to Dr. A.O.D. Willows, Director, Friday Harbor Laboratories, fur use of laboratory facilities.

PY - 1992/2/15

Y1 - 1992/2/15

N2 - Many cnidarians utilize green-fluorescent proteins (GFPs) as energy-transfer acceptors in bioluminescence. GFPs fluoresce in vivo upon receiving energy from either a luciferase-oxyluciferin excited-state complex or a Ca2+-activated photoprotein. These highly fluorescent proteins are unique due to the chemical nature of their chromophore, which is comprised of modified amino acid (aa) residues within the polypeptide. This report describes the cloning and sequencing of both cDNA and genomic clones of GFP from the cnidarian, Aequorea victoria. The gfp10 cDNA encodes a 238-aa-residue polypeptide with a calculated Mr of 26888. Comparsion of A. victoria GFP genomic clones shows three different restriction enzyme patterns which suggests that at least three different genes are present in the A. victoria population at Friday Harbor, Washington. The gfp gene encoded by the λGFP2 genomic clone is comprised of at least three exons spread over 2.6 kb. The nucleotide sequences of the cDNA and the gene will aid in the elucidation of structure-function relationships in this unique class of proteins.

AB - Many cnidarians utilize green-fluorescent proteins (GFPs) as energy-transfer acceptors in bioluminescence. GFPs fluoresce in vivo upon receiving energy from either a luciferase-oxyluciferin excited-state complex or a Ca2+-activated photoprotein. These highly fluorescent proteins are unique due to the chemical nature of their chromophore, which is comprised of modified amino acid (aa) residues within the polypeptide. This report describes the cloning and sequencing of both cDNA and genomic clones of GFP from the cnidarian, Aequorea victoria. The gfp10 cDNA encodes a 238-aa-residue polypeptide with a calculated Mr of 26888. Comparsion of A. victoria GFP genomic clones shows three different restriction enzyme patterns which suggests that at least three different genes are present in the A. victoria population at Friday Harbor, Washington. The gfp gene encoded by the λGFP2 genomic clone is comprised of at least three exons spread over 2.6 kb. The nucleotide sequences of the cDNA and the gene will aid in the elucidation of structure-function relationships in this unique class of proteins.

KW - Bioluminescence

KW - Cnidaria

KW - aequorin

KW - chromophore

KW - cloning

KW - energy transfer

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JO - Gene

JF - Gene

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Primary structure of the Aequorea victoria green-fluorescent protein

Abstract

Keywords

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