Determination of the binding domain of DDX3 with ALKBH5. (a) Schematic diagram of full-length DDX3 and the corresponding partial deletion constructs; summary of the results of interaction with ALKBH5 was also shown. (b) Deletion of N-terminal domain, Linker domain, Helicase domain, or the C-terminal domain of DDX3 showed interaction with the full-length ALKBH5, as examined with IP and co-IP. (c) The interaction was abolished when ATP domain of DDX3 was deleted, as examined with IP and co-IP. (d) ATP domain of DDX3 alone interacted with full-length ALKBH5, examined with IP and co-IP. All IP and co-IP were performed in triplicates, and representative results were shown.