JMJD5 is a human arginyl C-3 hydroxylase

Sarah E. Wilkins, Md. Saiful Islam, Joan M. Gannon, Suzana Markolovic, Richard J. Hopkinson, Wei Ge, Christopher J. Schofield () and Rasheduzzaman Chowdhury ()
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Sarah E. Wilkins: University of Oxford
Md. Saiful Islam: University of Oxford
Joan M. Gannon: University of Oxford
Suzana Markolovic: University of Oxford
Richard J. Hopkinson: University of Oxford
Wei Ge: University of Oxford
Christopher J. Schofield: University of Oxford
Rasheduzzaman Chowdhury: University of Oxford

Nature Communications, 2018, vol. 9, issue 1, 1-12

Abstract: Abstract 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.

Date: 2018
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DOI: 10.1038/s41467-018-03410-w

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