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. 2021 Jun 28;49(13):7740–7752. doi: 10.1093/nar/gkab542

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© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 3. — Biochemical functions of the SAP domain of SLX4. (A) The SAP domain of SLX4 enhances DNA binding of the SLX1–SLX4 complex. Fluorescence Polarization Assay (FPA) assessment of the binding of SLX1–SLX4 complexes with the indicated SLX4 fragments to 5′-flap DNA. The derived K_D values are displayed. (B) The SAP domain of SLX4 is required for efficient and accurate cleavage of DNA substrates. Top panel, schematics of truncation fragments of SLX4^SAP+CCD used for assessing the function of SAP domain; middle and bottom left panels, cleavage of HJ and 5′-flap DNA by complexes formed between SLX1 and the indicated SLX4 fragments, assessed by native gel electrophoresis, respectively; middle and bottom right panels, analysis of the indicated SLX4 mutant complexes by denatured gel electrophoresis, respectively. The SLX1 Y29F mutant complex with the F1 fragment of SLX4 is shown as a negative control.