Structural basis for the non-canonical nucleosome remodeling by ATRX.

Three human ATRX ATPase domain structures show a primed but autoinhibited conformation that is relieved by nucleosome binding, enabling ATP-dependent disassembly via a non-canonical site.

• Why it matters: ATRX is an Snf2-family remodeler needed for chromatin regulation and genome stability, yet how it is regulated and how it remodels nucleosomes has been unclear.
• What they did: The authors solved structures of the ATRX ATPase domain in free, nucleosome-bound, and histone-bound states, identifying nucleosome-triggered relief of autoinhibition and DNA contacts at SHL 5.5–7.
• The result: ATRX favors ATP-dependent nucleosome disassembly over sliding, and an ATRX histone-binding motif promotes disassembly and, with ASF1, tetrasome assembly; genome-wide data link ATRX to accessibility at intergenic regulatory elements independently of DAXX.

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