Reference: Turegun B, et al. (2018) Actin-related proteins regulate the RSC chromatin remodeler by weakening intramolecular interactions of the Sth1 ATPase. Commun Biol 1:1

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Abstract


The catalytic subunits of SWI/SNF-family and INO80-family chromatin remodelers bind actin and actin-related proteins (Arps) through an N-terminal helicase/SANT-associated (HSA) domain. Between the HSA and ATPase domains lies a conserved post-HSA (pHSA) domain. The HSA domain of STH1, the catalytic subunit of the yeast SWI/SNF-family remodeler RSC, recruits the RTT102-ARP7/9 heterotrimer. RTT102-ARP7/9 regulates RSC function, but the mechanism is unclear. We show that the pHSA domain interacts directly with another conserved region of the catalytic subunit, protrusion-1. RTT102-ARP7/9 binding to the HSA domain weakens this interaction and promotes the formation of stable, monodisperse complexes with DNA and nucleosomes. A crystal structure of RTT102-ARP7/9 shows that ATP binds to ARP7 but not ARP9. However, ARP7 does not hydrolyze ATP. Together, the results suggest that RTT102 and ATP stabilize a conformation of ARP7/9 that potentiates binding to the HSA domain, which releases intramolecular interactions within STH1 and controls DNA and nucleosome binding.

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Journal Article
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Turegun B, Baker RW, Leschziner AE, Dominguez R
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