Structural insights into histone exchange by human SRCAP complex.

ABSTRACT: Histone variant H2A.Z is found at promoters and regulates transcription. The ATP-dependent chromatin remodeler SRCAP complex (SRCAP-C) promotes the replacement of canonical histone H2A-H2B dimer with H2A.Z-H2B dimer. Here, we determined structures of human SRCAP-C bound to H2A-containing nucleosome at near-atomic resolution. The SRCAP subunit integrates a 6-subunit actin-related protein (ARP) module and an ATPase-containing motor module. The ATPase-associated ARP module encircles half of the nucleosome along the DNA and may restrain net DNA translocation, a unique feature of SRCAP-C. The motor module adopts distinct nucleosome binding modes in the apo (nucleotide-free), ADP-bound, and ADP-BeF_x-bound states, suggesting that ATPase-driven movement destabilizes H2A-H2B by unwrappin

SUBMITTER: Yu J 

PROVIDER: S-EPMC10853557 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature