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. 2021 Jun 18;12:3780. doi: 10.1038/s41467-021-24035-6

Fig. 3. PRMT1 physically interacts with and methylates METTL14.

Fig. 3

a List of the five most abundant proteins identified in the tandem affinity purification (TAP) pull down assay with METTL14 identified by LC–MS/MS using Mascot search engine in HeLa cells. b–c Co-IP of endogenous METTL14 (b) and PRMT1 (c) in HeLa cells. d Schematic of METTL14 truncations. MTD methyltransferase domain, NLS nuclear localization signal, RGG RGG repeats. e Western blot showing interactions of PRMT1 and ectopically expressed full-length or truncated METTL14 in HeLa cells. Representative figures of three independent replicates are shown. f In vitro methylation of R255me, R255, and R255K peptides by PRMT1. Representative figures of two independent replicates are shown. SAM S-Adenosyl-L-Methionine. Source data for (b), (c), (e) and (f) are provided as a Source Data file.