Figure 3 | Cell Discovery

Figure 3

From: C-terminal domains of histone demethylase JMJ14 interact with a pair of NAC transcription factors to mediate specific chromatin association

Figure 3

JMJ14 (Jumonji C (JmjC) domain-containing protein 14) interacts with NAC050 and NAC052 through its FYR (FYRN+FYRC) domain in vitro and in vivo. (a) The schematic representation of constructs used for yeast two hybrids. (b) The full-length JMJ14 interacts with NAC050 and NAC052 in yeast (left). Deletion of FYR domain completely abolishes the interaction between JMJ14 and NAC050/NAC052 while FYR domain alone could interact with NAC050/NAC052 in yeast (right). ‘-2’ indicates SD/-Trp-Leu medium, ‘-4’ indicates SD/-Trp-Leu-His-Ade medium with X-α-Gal. (c) Recombinant His-maltose binding protein-NAC050/052 interact with glutathione S-transferase (GST)-FYR directly but not GST in vitro. (d) JMJ14, but not JMJ14ΔFYR, was immunoprecipitated by anti-NAC detected by western blot (WB). JMJ14-HA refers to the PJMJ14::JMJ14-HA jmj14-1 transgenic lines and JMJ14ΔFYR-HA refers to the PJMJ14:: JMJ14ΔFYR-HA jmj14-1 transgenic lines. The red star and the red cross indicate JMJ14-HA and JMJ14ΔFYR-HA fusion proteins, respectively, detected by anti-HA.

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