[ PDB file ] [ PubMed link ]
It has been known for some time that the sidechains of several lysine residues in the transcription factor GATA1 can be modified by acetylation, but the function of these modifications has not been so clear. Our collaborator Gerd Blobel from the Children’s Hospital in Philadelphia has shown that, although acetylation doesn’t reduce the in vitro binding of GATA1 to DNA, acetylation of these lysines is essential for the localization of GATA1 to a chromatinized template. He more recently showed that acetylated GATA1 is recognized by Brd3. Together with Gerd, we have shown that the Brd3 bromodomain recognized a *doubly* acetylated GATA1 motif, and we have determined the structure of Brd3-bromodomain 1 bound to a GATA1 peptide containing two acetyllysine residues.