Primary structure of the Aequorea victoria green-fluorescent protein
- PMID: 1347277
- DOI: 10.1016/0378-1119(92)90691-h
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 Ca(2+)-activated phosphoprotein. 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 26,888. Comparison 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 lambda GFP2 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.
Similar articles
-
Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein.Biochemistry. 1993 Feb 9;32(5):1212-8. doi: 10.1021/bi00056a003. Biochemistry. 1993. PMID: 8448132
-
Green fluorescent protein: untapped potential in immunotechnology.Immunotechnology. 1995 Aug;1(2):83-6. doi: 10.1016/1380-2933(95)00011-9. Immunotechnology. 1995. PMID: 9373336 Review.
-
Green fluorescent protein.Photochem Photobiol. 1995 Oct;62(4):651-6. doi: 10.1111/j.1751-1097.1995.tb08712.x. Photochem Photobiol. 1995. PMID: 7480149 Review.
-
Deletion mapping of the Aequorea victoria green fluorescent protein.Gene. 1996;173(1 Spec No):39-44. doi: 10.1016/0378-1119(95)00692-3. Gene. 1996. PMID: 8707054
-
Characterization and use of green fluorescent proteins from Renilla mulleri and Ptilosarcus guernyi for the human cell display of functional peptides.J Protein Chem. 2001 Aug;20(6):507-19. doi: 10.1023/a:1012514715338. J Protein Chem. 2001. PMID: 11760126
Cited by
-
Opticool: Cutting-edge transgenic optical tools.PLoS Genet. 2024 Mar 22;20(3):e1011208. doi: 10.1371/journal.pgen.1011208. eCollection 2024 Mar. PLoS Genet. 2024. PMID: 38517915 Free PMC article. Review.
-
Breaking up the StayGold dimer yields three photostable monomers.Nat Methods. 2024 Mar 14. doi: 10.1038/s41592-024-02223-8. Online ahead of print. Nat Methods. 2024. PMID: 38485740 No abstract available.
-
The reckoning of chromosomal instability: past, present, future.Chromosome Res. 2024 Feb 17;32(1):2. doi: 10.1007/s10577-024-09746-y. Chromosome Res. 2024. PMID: 38367036 Review.
-
Chemical control of excited-state reactivity of the anionic green fluorescent protein chromophore.Commun Chem. 2024 Feb 5;7(1):25. doi: 10.1038/s42004-024-01099-1. Commun Chem. 2024. PMID: 38316834 Free PMC article.
-
A Monochromatically Excitable Green-Red Dual-Fluorophore Fusion Incorporating a New Large Stokes Shift Fluorescent Protein.Biochemistry. 2024 Jan 2;63(1):171-180. doi: 10.1021/acs.biochem.3c00451. Epub 2023 Dec 19. Biochemistry. 2024. PMID: 38113455 Free PMC article.
Publication types
MeSH terms
Substances
Associated data
- Actions
- Actions
- Actions
- Actions
- Actions
- Actions
- Actions
- Actions
- Actions
- Actions
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Miscellaneous
