Extended Data Fig. 8: PALB2 binding affinity for sdRNA is independent of Dicer or AGO1 and AGO2, but the recruitment of PALB2 and RAD52 to pause sites is, respectively, RAD52- and PALB2-dependent. | Nature

Extended Data Fig. 8: PALB2 binding affinity for sdRNA is independent of Dicer or AGO1 and AGO2, but the recruitment of PALB2 and RAD52 to pause sites is, respectively, RAD52- and PALB2-dependent.

From: BRCA1 and RNAi factors promote repair mediated by small RNAs and PALB2–RAD52

Extended Data Fig. 8

a, PALB2 and RAD52 genome-wide RIP analyses of sRNAs are shown as heat maps centred around the sdRNA peaks identified in Fig. 2. b, PALB2 and RAD52 RIP analyses of ACTB and CASP16P sdRNA binding in RAD52- and PALB2-depleted cells, respectively. Representative experiment showing the mean ± s.d. of the qPCR replicates. c, Representative RIP analysis showing the relative abundance of PALB2-bound ACTB or CASP16P sdRNAs (quantified by TaqMan and qPCR) after depletion of DICER1 or AGO1. d, e, PALB2 (d) and RAD52 (e) ChIP analyses showing ChIP antibody specificity as well as how PALB2 or RAD52 recruitment is influenced by PALB2 or RAD52 depletion (n = 2–4 and n = 2–3 biological replicates, respectively, for PALB2 and RAD52 ChIP). f, RAD52 ChIP analyses with or without depletion of GapmeR-directed ACTB or CASP16P sdRNA. ChIP results are shown as the mean ± s.e.m. fold change compared to the mock siRNA. Data were analysed by one-way (b, c) or two-way (d, e) ANOVA with post hoc Tukey HSD test or multiple t-test (f) and compared to the relevant control cells.

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