The histone acetyltransferase activity of ZmELP3 was analysed according to a previously described protocol with minor modifications (Xu et al., 2023 (link)). Vectors of Pro35S:ZmELP3A or Pro35S:ZmELP3B and Pro35S:ZmH3.2‐GFP were transformed into Agrobacterium strain GV3101, and then infiltrated into 5‐week‐old N. benthamiana leaves. After ground into powder by liquid nitrogen of the transfected tobacco leaves, the total proteins were extracted using IP buffer (10 mm Tris–HCl, pH 7.5, 0.5 mm EDTA, 150 mm NaCl, 0.5% Nonidet P‐40 and 1% protease inhibitor cocktail). After removing cellular debris, the supernatant was added to anti‐GFP magnetic beads (Beyotime) and incubated for 3 h at 4 °C. The beads were then washed five times with IP buffer. The extracted proteins were analysed using Western blotting and detected with anti‐H3 (Abcam, ab1791, 1 : 1000), anti‐ELP3 (Invitrogen, 702 669, 1 : 1000) and anti‐H3K14ac (Abcam, ab52946, 1 : 1000).