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An improved mRFP1 adds red to bimolecular fluorescence complementation

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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.

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Figure 1: Spectral properties of new mRFP1 mutants.
Figure 2: Bimolecular fluorescence complementation of mRFP1-Q66T fragments.

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Acknowledgements

We thank G. Coupland and M. Hülskamp for support, and M. Mutondo for critically reading the manuscript. The work was supported by grants from the Max Planck Society.

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Authors and Affiliations

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

    Guido Jach, Klaus Richter, Sabine Frings & Joachim F Uhrig

  2. Department of Botany III, University of Cologne, Gyrhofstr. 15, Cologne, D-50931, Germany

    Martina Pesch & Joachim F Uhrig

Authors
  1. Guido Jach
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  2. Martina Pesch
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  3. Klaus Richter
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  4. Sabine Frings
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  5. Joachim F Uhrig
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Corresponding authors

Correspondence to Guido Jach or Joachim F Uhrig.

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The authors declare no competing financial interests.

Supplementary information

Supplementary Fig. 1

Analysis of negative controls (PDF 1891 kb)

Supplementary Fig. 2

Analysis of homeodomain protein interactions (PDF 70 kb)

Supplementary Methods (PDF 105 kb)

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Jach, G., Pesch, M., Richter, K. et al. An improved mRFP1 adds red to bimolecular fluorescence complementation. Nat Methods 3, 597–600 (2006). https://doi.org/10.1038/nmeth901

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