Fig. 5: Binding of the HLB domain of Ioc3 to extranucleosomal DNA is required for ISW1a to bind dinucleosomes. | Nature Communications

Fig. 5: Binding of the HLB domain of Ioc3 to extranucleosomal DNA is required for ISW1a to bind dinucleosomes.

From: Dinucleosome specificity and allosteric switch of the ISW1a ATP-dependent chromatin remodeler in transcription regulation

Fig. 5: Binding of the HLB domain of Ioc3 to extranucleosomal DNA is required for ISW1a to bind dinucleosomes.

a The HLB domain of Ioc3 (red) was partially truncated as depicted to disrupt its binding to extranucleosomal or linker DNA. Ioc3 domains are shown in blue. b The crystal structure of truncated ISW1a with free DNA is shown and the region of HLB that was deleted in red6. The HSS domain of Isw1 (cyan) and Ioc3 (green) are shown. c Wild-type and mutant ISW1a with the C-terminal end of HLB deleted (ΔcHLB) were analyzed by SDS-PAGE and stained with Coomassie blue. d–g The interactions of ΔcHLB ISW1a with (d) 0N70, (e) 50(N1)50(N2)6 and (f) 43N33 nucleosomes or (g) wild-type ISW1a with 43N33 nucleosomes were analyzed by DNA footprinting with hydroxyl radicals. Black traces are nucleosome alone and red are the nucleosomes fully bound by wild-type or mutant ISW1a. DNA footprinting experiments had a minimum of 2–3 replicates with similar results as those depicted. Source data are provided as a Source Data file.

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