6lsd | pdb_00006lsd
Crystal Structure of YEATS domain of human YEATS2 in complex with H3K27bz peptide
Structural highlights
FunctionYETS2_HUMAN Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4.[1] Publication Abstract from PubMedHistone modifications and their functional readout serve as an important mechanism for gene regulation. Lysine benzoylation (Kbz) on histones is a recently identified acylation mark associated with active transcription. However, it remains to be explored whether putative readers exist to recognize this epigenetic mark. Here, our systematic binding studies demonstrated that the DPF and YEATS, but not the Bromodomain family members, are readers for histone Kbz. Co-crystal structural analyses revealed a 'hydrophobic encapsulation' and a 'tip-sensor' mechanism for Kbz readout by DPF and YEATS, respectively. Moreover, the DPF and YEATS family members display subtle yet unique features to create somewhat flexible engagements of different acylation marks. For instance, YEATS2 but not the other YEATS proteins exhibits best preference for Kbz than lysine acetylation and crotonylation due to its wider 'tip-sensor' pocket. The levels of histone benzoylation in cultured cells or in mice are upregulated upon sodium benzoate treatment, highlighting its dynamic regulation. In summary, our work identifies the first readers for histone Kbz and reveals the molecular basis underlying Kbz recognition, thus paving the way for further functional dissections of histone benzoylation. Histone benzoylation serves as an epigenetic mark for DPF and YEATS family proteins.,Ren X, Zhou Y, Xue Z, Hao N, Li Y, Guo X, Wang D, Shi X, Li H Nucleic Acids Res. 2021 Jan 11;49(1):114-126. doi: 10.1093/nar/gkaa1130. PMID:33290558[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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