The BioGRID | PUBLICATION VIEW

	Nat. Struct. Mol. Biol. May (2008); 15(5):469-76
The HSA domain binds nuclear actin-related proteins to regulate chromatin-remodeling ATPases-
Szerlong H, Hinata K, Viswanathan R, Erdjument-Bromage H, Tempst P, Cairns BR
Howard Hughes Medical Institute, Department of Oncological Sciences, Huntsman Cancer Institute, 2000 Circle of Hope, University of Utah, Salt Lake City, Utah 84112, USA-
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-
[PUBMED: 18408732]