Fig. 7: Kinetic model for H2A.Z deposition by SWR1C.
From: H2A.Z deposition by SWR1C involves multiple ATP-dependent steps
Initially, SWR1C binds to the linker-distal face of an asymmetric H2A-nucleosome, such as the +1 nucleosome adjacent to the NFR. SWR1C binding at SHL2 induces stress and transient dynamics at the nucleosomal DNA edge. While nucleosome-bound, SWR1C hydrolyzes ATP for an extended period of time to prime the nucleosomal substrate for H2A eviction (tprime), leading to more extensive unwrapping of nucleosomal DNA and transient deformations of the histone octamer. Sufficient priming allows SWR1C to rapidly perform its H2A to H2A.Z dimer exchange reaction on the nucleosome (tevict). The evicted H2A/H2B dimer remains associated with the SWR1C still bound to the exchanged nucleosome, until the SWR1C-H2A/H2B complex is released from the nucleosome through ATP hydrolysis (trelease).
