NMR spectroscopy uncovers direct interaction between BAF60A and p53.

The BRG1-associated factor 60A (BAF60A), an SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1, has been known to be important for transcriptional activation and inhibition through the alteration of the DNA nucleosome. Although the association between BAF60A and p53 plays a critical role in tumor suppression, the interaction mode is still unclear. Here, we report the detailed interactions between BAF60A and p53 by both NMR spectroscopy and pull-down analysis. Both N-terminal region (BAF60A^NR) and the SWIB domain (BAF60A^SWIB) of BAF60A directly interact with the tetramerization domain of p53 (p53^TET). NMR data show that Ile315, Met366, Ala388, and Tyr390 of BAF60A^SWIB are mostly involved in p53^TET binding. The calculated dissociation constant (K_D) value between BAF60A^SWIB and p53^TET revealed relatively weak binding affinity, at approximately 0.3 ± 0.065 mM. Our data will enhance detailed interaction mechanism to elucidate the molecular basis of p53-mediated integration via BAF60A interaction.

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