An improved mRFP1 adds red to bimolecular fluorescence complementation

Protein-protein interactions are fundamental to virtually every aspect of cellular functions. Blue, green and yellow bimolecular fluorescence complementation (BiFC) systems based on GFP and its variants allow the investigation of protein-protein interactions in vivo . We have developed the first red...

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Veröffentlicht in:	Nature methods 2006-08, Vol.3 (8), p.597-600
Hauptverfasser:	Jach, Guido, Pesch, Martina, Richter, Klaus, Frings, Sabine, Uhrig, Joachim F
Format:	Artikel
Sprache:	eng
Schlagworte:	Bioinformatics Biological Microscopy Biological Techniques Biomedical and Life Sciences Biomedical Engineering/Biotechnology brief-communication Cellular biology Color Fluorescence Fluorescence spectroscopy Gene Expression Profiling - methods Innovations Life Sciences Luminescent Proteins - analysis Luminescent Proteins - chemistry Luminescent Proteins - metabolism Microscopy, Fluorescence, Multiphoton - methods Physiological aspects Protein Interaction Mapping - methods Protein-protein interactions Proteins Proteomics R&D Recombinant Fusion Proteins - analysis Red Fluorescent Protein Reproducibility of Results Research & development Sensitivity and Specificity Spectrometry, Fluorescence - methods
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Beschreibung
Zusammenfassung:	Protein-protein interactions are fundamental to virtually every aspect of cellular functions. Blue, green and yellow bimolecular fluorescence complementation (BiFC) systems based on GFP and its variants allow the investigation of protein-protein interactions in vivo . We have developed the first red BiFC system based on an improved monomeric red fluorescent protein (mRFP1-Q66T), expanding the range of possible applications for BiFC.
ISSN:	1548-7091 1548-7105
DOI:	10.1038/nmeth901