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One HAT size fits all?

Nature Structural Biology volume 8, pages 8–10 (2001)Cite this article

The structure of yeast Esa1 suggests that different families of histone acetyltransferases employ similar mechanisms of substrate binding and catalysis. Deletion studies used to optimize the protein for crystallization also emphasize the importance of Esa1 function within a larger, multiprotein HAT complex.

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Figure 1: A common mode of CoA binding in the Gcn5, Esa1 and Hat1 crystal structures.
Figure 2: Gcn5 binding of histone H3 suggests a potential peptide binding groove in the Esa1 structure.

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  1. the Department of Biochemistry & Molecular Biology, Center for Gene Regulation, The Pennsylvania State University, University Park, Pennsylvania, 16802-1014, USA

    Song Tan

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Tan, S. One HAT size fits all?. Nat Struct Mol Biol 8, 8–10 (2001). https://doi.org/10.1038/83098

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