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Titolo:
FLUORESCENCE RESONANCE ENERGY-TRANSFER BETWEEN BLUE-EMITTING AND RED-SHIFTED EXCITATION DERIVATIVES OF THE GREEN FLUORESCENT PROTEIN
Autore:
MITRA RD; SILVA CM; YOUVAN DC;
Indirizzi:
KAIROS SCI INC,BLDG 62,3350 SCOTT BLVD SANTA CLARA CA 95054 KAIROS SCI INC SANTA CLARA CA 95054 PALO ALTO INST MOLEC MED MT VIEW CA 94043
Titolo Testata:
Gene
fascicolo: 1, volume: 173, anno: 1996,
pagine: 13 - 17
SICI:
0378-1119(1996)173:1<13:FREBBA>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
MUTAGENESIS; FRET;
Keywords:
FRET; AEQUOREA VICTORIA; FLUORESCENT PROTEINS; FACTOR X(A);
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
18
Recensione:
Indirizzi per estratti:
Citazione:
R.D. Mitra et al., "FLUORESCENCE RESONANCE ENERGY-TRANSFER BETWEEN BLUE-EMITTING AND RED-SHIFTED EXCITATION DERIVATIVES OF THE GREEN FLUORESCENT PROTEIN", Gene, 173(1), 1996, pp. 13-17

Abstract

We report fluorescent resonance energy transfer (FRET) between two linked variants of the green fluorescent protein (GFP). The C terminus of a red-shifted variant of GFP (RSGFP4) is fused to a flexible polypeptide linker containing a Factor X(a) protease cleavage site. The C terminus of this linker is in turn fused to the N terminus of a blue variant of GFP (BFP5), The gene product has spectral properties that suggest energy transfer is occurring from BFP5 to RSGFP4. Upon incubation with Factor X(a), the protein is cleaved, and the two fluorescent proteins dissociate. This is accompanied by a marked decrease in energy transfer. The RSGFP4::BFP5 fusion protein demonstrates the feasibility ofusing FRET between two GFP derivatives as a tool to monitor protein-protein interactions; in addition, this construct may find applicationsas an intracellular screen for protease inhibitors.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 01:47:37