Fig. 3: PARP1 avidly binds nucleosome particles in the absence of DNA damage. | Nature Communications

Fig. 3: PARP1 avidly binds nucleosome particles in the absence of DNA damage.

From: Nucleosome unwrapping and PARP1 allostery drive affinities for chromatin and DNA breaks

Fig. 3: PARP1 avidly binds nucleosome particles in the absence of DNA damage.

a A schematic showing the strategy for ligating reconstituted 601 nucleosomes into the DNA handles kit (LUMICKS), as well as a resultant 2D scan demonstrating colocalization between the Cy3 signal of the nucleosome and the ATTO 647 N dye (represented by red A). b Representative kymograph of WT PARP1 engaging fully wrapped nucleosomes at low DNA tension, with the distal (weak) arm marked in orange (from PDB 4JJN). CRTD and CGTD plots shown on the right, as well as resultant affinity measurement. c At tensions > 5 pN, the distal arm (orange) unwraps, see model shown. A representative kymograph is shown, as is the CRTD, CGTD, and affinity measurement. Nucleosome models created in BioRender. Schaich, M. (2025) https://BioRender.com/du7zz94.

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