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JMJD5 is a human arginyl C-3 hydroxylase

Author

Listed:
  • 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
    University of Leicester)

  • Wei Ge

    (University of Oxford)

  • Christopher J. Schofield

    (University of Oxford)

  • Rasheduzzaman Chowdhury

    (University of Oxford
    Clark Center)

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.

Suggested Citation

  • Sarah E. Wilkins & Md. Saiful Islam & Joan M. Gannon & Suzana Markolovic & Richard J. Hopkinson & Wei Ge & Christopher J. Schofield & Rasheduzzaman Chowdhury, 2018. "JMJD5 is a human arginyl C-3 hydroxylase," Nature Communications, Nature, vol. 9(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-03410-w
    DOI: 10.1038/s41467-018-03410-w
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