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Fig. S1
Promiscuous interaction between Her1, Her7, and Hes6. GFP-tagged Her1 (left), Her7 (middle), or Hes6 (right) was co-expressed with different mCherry-tagged proteins in an in vitro transcription-translation system as indicated. GFP-tagged proteins were purified by immunoprecipitation using a GFP-antibody and transferred to membranes. Probing for mCherry-tagged proteins (upper panels) reveals that all proteins containing a basic helix-loop-helix domain (i.e., MyoD, Her1, Her7, and Hes6) are co-purified with the GFP-tagged protein significantly stronger than the negative control PPARγ but that there is little difference in co-purification efficiency between different bHLH proteins. This indicates that the bHLH proteins investigated here interact promiscuously. IP, immunoprecipitation; IB, immunoblotting.