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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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Both dmJMJD7 and hsJMJD7 are dimeric 2OG-oxygenases. Structural analysis of the oligomerization domains of Drosophila (A) and human (B) JMJD7 reveals a conserved role for α-helices in oligomerization between monomers, which is reminiscent of dimerization in FIH and TYW5^2,3, though the nature of the interactions differs. While FIH and TYW5 employ C-terminally located α-helices for dimerizations, JMJD7 dimerizes via a mode involving both N- (α1 and α2) and C- (α9) terminal α-helical regions (see text for details).