6axj
From Proteopedia
Crystal structure of the Yaf9 YEATS domain bound to H3K27ac
Structural highlights
Function[AF9_YEAST] Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4 and H2A. The NuA4 complex is also involved in DNA repair. Yaf9 may also be required for viability in conditions in which the structural integrity of the spindle is compromised.[1] [2] [3] [4] [5] Publication Abstract from PubMedYaf9 is an integral part of the NuA4 acetyltransferase and the SWR1 chromatin remodeling complexes. Here, we show that Yaf9 associates with acetylated histone H3 with high preference for H3K27ac. The crystal structure of the Yaf9 YEATS domain bound to the H3K27ac peptide reveals that the sequence C-terminal to K27ac stabilizes the complex. The side chain of K27ac inserts between two aromatic residues, mutation of which abrogates the interaction in vitro and leads in vivo to phenotypes similar to YAF9 deletion, including loss of SWR1-dependent incorporation of variant histone H2A.Z. Our findings reveal the molecular basis for the recognition of H3K27ac by a YEATS reader and underscore the importance of this interaction in mediating Yaf9 function within the NuA4 and SWR1 complexes. Yaf9 subunit of the NuA4 and SWR1 complexes targets histone H3K27ac through its YEATS domain.,Klein BJ, Ahmad S, Vann KR, Andrews FH, Mayo ZA, Bourriquen G, Bridgers JB, Zhang J, Strahl BD, Cote J, Kutateladze TG Nucleic Acids Res. 2017 Nov 14. pii: 4626774. doi: 10.1093/nar/gkx1151. PMID:29145630[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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