Fig. 4: Activation mechanism of the DREN nuclease domain.
From: Target DNA-induced filament formation and nuclease activation of SPARDA complex
a Cryo-EM map of the substrate-bound NbaSPARDA complex, with the DREN tetramer shown alongside in zoomed-in view. b Interaction details between the DREN tetramer and the filament (left), and interaction details between the main chains of DREN and the phosphate backbone of the substrate DNA (right). Bridging loops were colored in black. c Detailed structure of the DREN domain, and its interaction with the substrate ssDNA. d Interaction details on the α1–α1 interface. e Interaction details on the β1β2–β1β2 interface. f FQ assay to evaluate the effect of DREN-related mutants on collateral nuclease activity. FQ assay was performed in triplicate, and the error bars represent the standard deviations. DREN tetramer disruption mutant: N17A/E13A/R20A/R33A/Q29A/E45A/D31A.
