Visualizing protein interactions by bimolecular fluorescence complementation in Xenopus

Yasushi Saka, Anja I Hagemann, James C Smith

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)


Bimolecular fluorescence complementation (BiFC) provides a simple and direct way to visualise protein-protein interactions in vivo and in real-time. In this article, we describe methods by which one can implement this approach in embryos of the South African claw-toed frog Xenopus laevis. We have made use of Venus, an improved version of yellow fluorescent protein (YFP), so as to achieve rapid detection of protein interactions. To suppress spontaneous interactions between the N- and C-terminal fragments of Venus, a point mutation (T153M) was introduced into the N-terminal fragment. We have used this reagent to monitor signalling by members of the transforming growth factor type beta family in cells of the Xenopus embryo.
Original languageEnglish
Pages (from-to)192-195
Number of pages4
Issue number3
Early online date27 Jun 2008
Publication statusPublished - Jul 2008


  • Activins
  • Animals
  • Embryo, Nonmammalian
  • Fluorescent Dyes
  • Gene Transfer Techniques
  • Kinetics
  • Luminescent Proteins
  • Microscopy, Fluorescence
  • Protein Interaction Mapping
  • Recombinant Fusion Proteins
  • Research Design
  • Smad2 Protein
  • Smad4 Protein
  • Xenopus Proteins
  • Xenopus laevis


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