ChIP-seq of HA-METTL14 in HepG2 cells

The METTL3-METTL14 heterodimer is the core component of the N6-methyltransferase complex (MTC) that catalyzes methylation of adenosine residues at the N(6) position of RNA. As the non-catalytic subunit of the MTC, METTL14 functions as the RNA-binding scaffold that recognizes the RNA substrate. We found METTL14 could interacte with chromatin through recognition of H3K36me3. ChIP-seq with HA-tagged METTL14 using an HA antibody identified 300 peaks in HepG2 cells, among which 53% peaks were located in the gene body and only 3% peaks were located in the promoter. The binding sites of METTL14 on chromatin correlate with that of H3K36me3.To investigat whether this interaction is Pol II dependent, we treated cells with a Pol II inhibitor 5,6-Dichlorobenzimidazole 1-ß-D-ribofuranoside (DRB) for a short time. Interestingly, we found the interaction of METTL14 with chromatin in gene body region was not affected by DRB treatment . Overall design: ChIP-seq using HA antibody in HepG2 cells with HA-METTL14 overexpression