Fig. 5: Mutating key residues in hnRNP L and SETD2 disrupts their in vitro and in vivo binding. | Nature Communications

Fig. 5: Mutating key residues in hnRNP L and SETD2 disrupts their in vitro and in vivo binding.

From: Structural basis of the interaction between SETD2 methyltransferase and hnRNP L paralogs for governing co-transcriptional splicing

Fig. 5: Mutating key residues in hnRNP L and SETD2 disrupts their in vitro and in vivo binding.

a ITC fitting curves of hnRNP L RRM2 WT and mutants with SETD22167–2192 peptide are shown. b, d, e Western blotting and silver staining of affinity-purified complexes of Halo-SETD2C WT and its mutants. In (b), mCherry-HA-hnRNP L proteins were used as prey. * denotes non-specific band. The experiment was repeated four times all yielding similar results. Source data are provided as a Source Data file. c, f ITC fitting curves of hnRNP L RRM2 with SETD2 peptides. For the arithmetic mean of KD values of the three independent experiments and the thermodynamic parameters see Supplementary Table 1. All ITC binding curves are shown in Supplementary Table 2.

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