Abstract
We identify the helicase-SANT–associated (HSA) domain as the primary binding platform for nuclear actin-related proteins (ARPs) and actin. Individual HSA domains from chromatin remodelers (RSC, yeast SWI-SNF, human SWI-SNF, SWR1 and INO80) or modifiers (NuA4) reconstitute their respective ARP–ARP or ARP–actin modules. In RSC, the HSA domain resides on the catalytic ATPase subunit Sth1. The Sth1 HSA is essential in vivo, and its omission causes the specific loss of ARPs and a moderate reduction in ATPase activity. Genetic selections for arp suppressors yielded specific gain-of-function mutations in two new domains in Sth1, the post-HSA domain and protrusion 1, which are essential for RSC function in vivo but not ARP association. Taken together, we define the role of the HSA domain and provide evidence for a regulatory relationship involving the ARP–HSA module and two new functional domains conserved in remodeler ATPases that contain ARPs.
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Acknowledgements
We thank J. Wittmeyer and A. Saha (Cairns laboratory) for plasmids, strains and expertise on protein purification. We thank J. Shaw, D. Close, M. Kasten, T. Parnell and J. Lenkart (all University of Utah) for reagents and advice. We thank W. Wang (US National Institutes of Health (NIH)) and M. Cole (Dartmouth University) for antibodies and plasmids, P. Hollenhorst and C. Foulds (University of Utah) for cell culture reagents and advice. This work was supported by the NIH (GM60415 to B.R.C., and support of H.S.), CA24014 for core facilities, and the Howard Hughes Medical Institute (support of B.R.C. and K.H.).
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H.S., K.H. and B.R.C. designed and interpreted experiments; H.S. and K.H. executed experiments and generated figures; R.V., H.S. and B.R.C. isolated and characterized sth1 alleles.; P.T. and H.E.-B. performed MS analysis; B.R.C., H.S. and K.H. wrote the manuscript.
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Szerlong, H., Hinata, K., Viswanathan, R. et al. The HSA domain binds nuclear actin-related proteins to regulate chromatin-remodeling ATPases. Nat Struct Mol Biol 15, 469–476 (2008). https://doi.org/10.1038/nsmb.1403
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DOI: https://doi.org/10.1038/nsmb.1403
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