An improved mRFP1 adds red to bimolecular fluorescence complementation

Guido Jach; Martina Pesch; Klaus Richter; Sabine Frings; Joachim F Uhrig

doi:10.1038/nmeth901

An improved mRFP1 adds red to bimolecular fluorescence complementation

Nat Methods. 2006 Aug;3(8):597-600. doi: 10.1038/nmeth901.

Authors

Guido Jach¹, Martina Pesch, Klaus Richter, Sabine Frings, Joachim F Uhrig

Affiliation

¹ Max Planck Institute for Plant Breeding Research, Department of Plant Developmental Biology, Carl von Linne Weg 10, D-50829 Cologne, Germany. jach@mpiz-koeln.mpg.de

PMID: 16862132
DOI: 10.1038/nmeth901

Abstract

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.

Publication types

Comparative Study
Evaluation Study
Research Support, Non-U.S. Gov't

MeSH terms

Gene Expression Profiling / methods*
Luminescent Proteins / analysis
Luminescent Proteins / chemistry*
Luminescent Proteins / metabolism*
Microscopy, Fluorescence, Multiphoton / methods*
Protein Interaction Mapping / methods*
Recombinant Fusion Proteins / analysis*
Red Fluorescent Protein
Reproducibility of Results
Sensitivity and Specificity
Spectrometry, Fluorescence / methods*

Substances

Luminescent Proteins
Recombinant Fusion Proteins