Journal article
Conservation of the unusual dimeric JmjC fold of JMJD7 from Drosophila melanogaster to humans
- Abstract:
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The JmjC family of 2-oxoglutarate dependent oxygenases catalyse a range of hydroxylation and demethylation reactions in humans and other animals. Jumonji domain-containing 7 (JMJD7) is a JmjC (3S)-lysyl-hydroxylase that catalyses the modification of Developmentally Regulated GTP Binding Proteins 1 and 2 (DRG1 and 2); JMJD7 has also been reported to have histone endopeptidase activity. Here we report biophysical and biochemical studies on JMJD7 from Drosophila melanogaster (dmJMJD7). Notably, crystallographic analyses reveal that the unusual dimerization mode of JMJD7, which involves interactions between both the N- and C-terminal regions of both dmJMJD7 monomers and disulfide formation, is conserved in human JMJD7 (hsJMJD7). The results further support the assignment of JMJD7 as a lysyl hydroxylase and will help enable the development of selective inhibitors for it and other JmjC oxygenases.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, pdf, 5.0MB, Terms of use)
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- Publisher copy:
- 10.1038/s41598-022-10028-y
Authors
- Publisher:
- Springer Nature
- Journal:
- Scientific Reports More from this journal
- Volume:
- 12
- Article number:
- 6065
- Publication date:
- 2022-04-11
- Acceptance date:
- 2022-03-30
- DOI:
- EISSN:
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2045-2322
- Pmid:
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35410347
- Language:
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English
- Keywords:
- Pubs id:
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1255291
- Local pid:
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pubs:1255291
- Deposit date:
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2023-08-07
Terms of use
- Copyright holder:
- Chowdhury et al.
- Copyright date:
- 2022
- Rights statement:
- Copyright © 2022, The Author(s). 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/.
- Notes:
- This research was funded in whole, or in part, by the Wellcome Trust [Grant No. 106244/Z/14/Z]. For the purpose of open access, the author has applied a CC BY public copyright license to any Author Accepted Manuscript version arising from this submission. We thank the editorial staff for very effcient processing of the manuscript.
- Licence:
- CC Attribution (CC BY)
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