Fig. 2: NRP proteins physically interact with H2A and H2A.Z in vivo.
From: NAP1-RELATED PROTEIN1 and 2 negatively regulate H2A.Z abundance in chromatin in Arabidopsis
a and b α-H2A.Z co-immunopurification assays; α-H2A.Z immunoprecipitation lanes (=H2A.Z IP) show co-purification of H2A.Z with NRP1 (a) and NRP2 (b). c α-H2A co-immunopurification assays; α-H2A immunoprecipitation lanes (=H2A IP), show co-purification of H2A with NRP1 and NRP2. We show empty beads as a negative control. d NRPs co-immunopurification assays; α-Myc immunoprecipitation lanes (=Myc IP) show co-purification of NRP1 and NRP2 with both unmodified and monoubiquitinated H2A.Z. For each Western blot, the antibody used for detection is indicated either at the bottom, in the case of a and b, or to the right, in the case of c and d. In all cases, protein extracts from the same plants are included to confirm the identity of the co-precipitating band (=Input). We included ARP6 as a positive control. All co-immunopurification assays were repeated with similar results. Source data are provided as a Source Data file.
