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. 2022 Apr 11;12:6065. doi: 10.1038/s41598-022-10028-y

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© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Lysyl hydroxylation sites in DRG1 and 2. (A) JMJD7-catalysed (3S)-lysyl hydroxylation. (B) Views from a crystal structure of Rbg1.Tma46 complex (the yeast homologue of human DRG1.DFRP1, PDB: 4A9A) highlighting the hydroxylation site. All DRG orthologues, including Rbg1, contain three additional domains (HTH, S5D2L and TGS) surrounding the GTPase domain. JMJD7 hydroxylates a highly conserved lysine residue at the apex of the DRG HTH domain (boxed yellow; see Figs. S1b and S2a for an alignment of DRG orthologues). (C) Views from the cryo-EM structure of yeast 80S ribosome bound to Rbg1.Tma46 complex (PDB: 7RR5, EMD-24652) showing molecular interactions between Rbg1 and the ribosomal A-site tRNA (for simplicity, the rest of the ribosome is not shown)¹⁴. The figure shows superimposed views of the Rbg1.Tma46 complexes in the free (PDB: 4A9A, colour coded as in (B) and ribosome-bound (PDB: 7RR5, golden-yellow) forms revealing conformational changes, particularly involving the Rbg1-TGS domain and Tma46 on ribosome binding. Given that the target lysine sidechain is in close contact with A-site tRNA, hydroxylation may affect interactions with the ribosome.