Structural basis of nucleosome recognition by the human NuA4/TIP60 acetyltransferase complex

The human NuA4/TIP60 (TIP60-C) HAT module structure bound to a nucleosome shows cooperative positioning of its catalytic center on the nucleosome surface, anchored to the acidic patch and linker DNA.

• Why it matters: TIP60-C is a key regulator of chromatin accessibility and genome stability, but the molecular way its catalytic HAT module engages nucleosomes was unclear.
• What they did: The authors solved the structure of the human TIP60-C HAT module in complex with a nucleosome, identifying how TIP60, EPC1, ING3, and MEAF6 assemble a binding architecture.
• The result: The structure reveals an intramolecular interaction involving the TIP60 N-terminal Tudor domain that suggests a mechanism for autoregulation of HAT activity, providing a basis for understanding metazoan chromatin modification.

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