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. 2020 Feb 26;11:1067. doi: 10.1038/s41467-020-14893-x

Fig. 1. NMT1 and NMT2 have lysine transferase activity and can modify ARF6 on K3.

Fig. 1

a Lysine steric properties resemble those of N-terminal glycine. b The alignment of the N-terminal sequences of human ARFs reveals a unique lysine residue in ARF6. c Monitoring NMT1 in vitro reactions on different ARF6 peptides using LC-MS. Total ion chromatograms searched for the substrate and product ions are shown. d HPLC separation of NMT reaction on ARF6 WT N-terminal peptide reveals mostly glycine myristoylated product. e NMT reaction with ARF6 WT protein and Alk12-CoA generates several modified species. Shown are in-gel fluorescence and FLAG western blot after TAMRA azide conjugation via click chemistry. f Simulated annealing omit 2FO–FC map (at 1.2 σ) surrounding the myristoyl-KVLSKIF product in NMT2. Peptide: cyan, Lys3: pink, myristoyl: orange. g Myristoyl–peptide and CoA products bound to chain A in the NMT1 myristoyl-AcKVLSKIF structure. The 1.0 σ 2FO–FC electron density map around the ligands is shown (blue mesh). h Comparison with PDB structure 509V (black), NMT1 containing myristoyl-glycine peptide product. i Model showing that NMT1 and NMT2 enzymes can modify G2, K3 of ARF6, or both.