BDF1 is a protein that possesses two bromodomains (shown in red and blue), two phosphorylation domains (not shown) and an extra terminal domain (not shown), that is involved in chromatin-remodelling, playing an important role in transcription regulation and chromatin signalling(1). It has been identified as a transcription factor through recruitment of Taf6/7, and subsequently TFIID, involved in the expression of genes including shRNA(2,3). More recently, studies have revealed that the bromodomains are necessary for the expression of meiotic specific genes, meiotic progression and thus, sporulation(4). BDF1 has also shown to associate with the SWR complex, which is responsible for incorporating the H2A.Z histone variant into chromatin(4). Lastly, Sawa et al. (2004) demonstrated that protein kinase CK2 phosphorylates Bdf-1, and this may regulate its functions(2).
This model shows the crystal structure of BDF-1 (pale orange), highlighting important tyrosine residues (white).
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