Cyclic-AMP-response element-binding protein (CREB)-binding protein, (CBP), and its paralog p300 are histone acetyl transferases playing a critical role in embryonic development, cell growth control, division as well as homeostasis. Via its Taz2 domain, they interact with multiple transcription factors to regulate gene expression. These transcription factors include CCAAT-enhancer-binding proteins, the C/EBP family. Through transactivation domain (TAD), C/EBPs recruit the co-activators (p300, CBP) that open up chromatin structure and mediate its phosphorylation through the recruitment of specific kinases. C/EBPβ binds to the closed chromatin and acts as a pioneering factor for initiating tissue-specific gene expression at several promoters. Here, we present the detailed structural characterization of the C/EBPβ interaction with CBP.
This work is supported by the Charles University Grant Agency (grant No. 227020).