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Titolo:
WAVELENGTH MUTATIONS AND POSTTRANSLATIONAL AUTOXIDATION OF GREEN FLUORESCENT PROTEIN
Autore:
HEIM R; PRASHER DC; TSIEN RY;
Indirizzi:
UNIV CALIF SAN DIEGO,HOWARD HUGHES MED INST LA JOLLA CA 92093 UNIV CALIF SAN DIEGO,HOWARD HUGHES MED INST LA JOLLA CA 92093 USDA,OTIS METHODS DEV CTR,ANIM & PLANT HLTH INSPECT SERV OTIS AIR NATL GUARD BASE MA 02542
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 26, volume: 91, anno: 1994,
pagine: 12501 - 12504
SICI:
0027-8424(1994)91:26<12501:WMAPAO>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
MUTAGENESIS; YEAST;
Keywords:
AEQUOREA VICTORIA; BLUE FLUORESCENT PROTEIN; ESCHERICHIA COLI; IMIDAZOLIDINONE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
20
Recensione:
Indirizzi per estratti:
Citazione:
R. Heim et al., "WAVELENGTH MUTATIONS AND POSTTRANSLATIONAL AUTOXIDATION OF GREEN FLUORESCENT PROTEIN", Proceedings of the National Academy of Sciences of the United Statesof America, 91(26), 1994, pp. 12501-12504

Abstract

The green fluorescent protein (GFP) of the jellyfish Aequorea victoria is an unusual protein with strong visible absorbance and fluorescence from a p-hydroxybenzylidene-imidazolidinone chromophore, which is generated by cyclization and oxidation of the protein's own Ser-Tyr-Gly sequence at positions 65-67. Cloning of the cDNA and heterologous expression of fluorescent protein in a wide variety of organisms indicate that this unique posttranslational modification must be either spontaneous or dependent only on ubiquitous enzymes and reactants. We report that formation of the final fluorophore requires molecular oxygen and proceeds with a time constant (approximate to 4 hr at 22 degrees C andatmospheric pO(2)) independent of dilution, implying that the oxidation does not require enzymes or cofactors. GFP was mutagenized and screened for variants with altered spectra. The most striking mutant fluoresced blue and contained histidine in plate of Tyr-66. The availability of two visibly distinct colors should significantly extend the usefulness of GFP in molecular and cell biology by enabling in vivo visualization of differential gene expression and protein localization and measurement of protein association by fluorescence resonance energy transfer.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 23:19:23