In participation of transcriptional regulation, transcription factors (TFs) interact with several other proteins. Here, we identified 7233 and 2176 protein-protein interactions for 110 different human TFs through proximity-dependent biotinylation (BioID) and affinity purification mass spectrometry (AP-MS), respectively. The BioID analysis resulted more high-confident interactions, highlighting the transient and dynamic nature of many of the TF interactions.
Using clustering and correlation analyses, we identified subgroups of TFs associated with specific biological functions, such as RNA-splicing, actin signalling or chromatin remodeling. We also observed 203 TF-TF interactions, of which 175 were interactions with Nuclear Factor 1 (NFI) -family members, indicating uncharacterized cross-talk between NFI signalling and numerous other TF signalling. Moreover, TF interactions with basal transcription machinery were mainly observed through TFIID and SAGA complexes.
This study, not only, provides a rich resource of human TF interactions, but also act as starting point directing future studies aimed at understanding TF mediated transcription.