The HSA domain binds nuclear actin-related proteins to regulate chromatin-remodeling ATPases Journal Article


Authors: Szerlong, H.; Hinata, K.; Viswanathan, R.; Erdjument-Bromage, H.; Tempst, P.; Cairns, B. R.
Article Title: The HSA domain binds nuclear actin-related proteins to regulate chromatin-remodeling ATPases
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. © 2008 Nature Publishing Group.
Keywords: controlled study; gene mutation; nonhuman; protein domain; actin; cell protein; protein binding; enzyme activity; regulatory mechanism; transcription regulation; amino acid sequence; molecular sequence data; saccharomyces cerevisiae; sequence alignment; chromatin; protein structure, tertiary; helicase; saccharomyces cerevisiae proteins; catalysis; actins; adenosine triphosphatase; enzyme subunit; adenosine triphosphatases; chromatin assembly and disassembly; genetic selection; cytoskeletal proteins; protein swi; transcription factor snf; actin related protein; actin related protein 7; actin related protein 9; protein ino80; protein sth1
Journal Title: Nature Structural and Molecular Biology
Volume: 15
Issue: 5
ISSN: 1545-9993
Publisher: Nature Publishing Group  
Date Published: 2008-05-01
Start Page: 469
End Page: 476
Language: English
DOI: 10.1038/nsmb.1403
PUBMED: 18408732
PROVIDER: scopus
PMCID: PMC2810487
DOI/URL:
Notes: --- - "Cited By (since 1996): 32" - "Export Date: 17 November 2011" - "CODEN: NSMBC" - "Source: Scopus"
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  1. Paul J Tempst
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