Journal article
JMJD5 is a human arginyl C-3 hydroxylase
- Abstract:
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Oxygenase catalysed post-translational modifications of basic protein residues including lysyl hydroxylations and Nε-methyl lysyl demethylations have important cellular roles. Jumonji-C (JmjC) domain-containing protein 5 (JMJD5), which genetic studies reveal is essential in animal development, is reported as a histone Nε-methyl lysine demethylase (KDM). Here we report how extensive screening with peptides based on JMJD5 interacting proteins led to the finding that JMJD5 catalyses stereoselective C-3 hydroxylation of arginine-residues in sequences from human regulator of chromosome condensation domain-containing protein 1 (RCCD1) and ribosomal protein S6 (RPS6). High-resolution crystallographic analyses reveal overall fold, active site and substrate binding/ product release features supporting the assignment of JMJD5 as an arginine hydroxylase rather than a KDM. The results will be useful in the development of selective oxygenase inhibitors for the treatment of cancer and genetic diseases.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, pdf, 311.8KB, Terms of use)
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- Publisher copy:
- 10.1038/s41467-018-03410-w
Authors
- Publisher:
- Springer Nature
- Journal:
- Nature Communications More from this journal
- Volume:
- 9
- Article number:
- 1180
- Publication date:
- 2018-03-21
- Acceptance date:
- 2018-03-05
- DOI:
- EISSN:
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2041-1723
- ISSN:
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2041-1723
- Pubs id:
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pubs:830024
- UUID:
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uuid:4b6981ff-7976-4647-a72b-bdd6419b5a13
- Local pid:
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pubs:830024
- Deposit date:
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2018-03-19
- ARK identifier:
Terms of use
- Copyright holder:
- Wilkins et al
- Copyright date:
- 2018
- Notes:
-
© 2018 Author(s); published by Macmillan Publishers Limited, part of Springer Nature under a Creative Commons Attribution 4.0 International License.
Note: an erratum exists for this article, originally published and available at: https://doi.org/10.1038/s41467-018-04196-7
- Licence:
- CC Attribution (CC BY)
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