Figure 3 - The combinatorial and dynamic nature of covalent modifications to the histone H3 N terminus, highlighting the role of 2OG oxygenases, and their role in introducing diversity into peptide-derived secondary metabolites.

(a) Identified modifications to part of the N terminus of histone H3 and their interplay^{19, 20}. Me, methylation (blue); Ac, acetylation; For, formylation; Cit, citrulline residue; P, phosphorylation. Arrowheads and bars, positive (green) and negative (red) effects, respectively, of one modification on occurrence of another. (b) Human 2OG oxygenases reported to modify histone N termini and residue specificity^{3, 19, 20, 22, 24, 30}. FBXL10/11, F-box and leucine-rich repeat proteins 10 and 11; JHDM2, jumonji histone demethylase 2 type; JMJD2/3/6, jumonji domain–containing protein 2, 3 and 6 type; JARID1, jumonji (A+T)-rich interactive domain 1 type; UTX, ubiquitously transcribed tetratricopeptide repeat gene X chromosome linked; sym and asym, symmetric and asymmetric. (c) Diversity-enhancing role of 2OG oxygenases in the daptomycin-like calcium-dependent antibiotic²⁹ CDA3 and etamycin⁴ biosynthesis. AsnO, asparagine hydroxylase (see Fig. 2c); P4H, proline (4R)-hydroxylase from Streptomyces griseoviridus P8648.