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JMJD5 is a human arginyl C-3 hydroxylase.

Nat Commun. 2018 Mar 21;9(1):1180
Sarah E Wilkins 1 , Md Saiful Islam 1 , Joan M Gannon 1 , Suzana Markolovic 1 , Richard J Hopkinson 2 , Wei Ge 1 , Christopher J Schofield 3 , Rasheduzzaman Chowdhury 4
Sarah E Wilkins 1 , Md Saiful Islam 1 , Joan M Gannon 1 , Suzana Markolovic 1 , Richard J Hopkinson 2 , Wei Ge 1 , Christopher J Schofield 3 , Rasheduzzaman Chowdhury 4
+ et al

[No authors listed]

Author information
  • 1 The Department of Chemistry, University of Oxford, Mansfield Road, Oxford, OX1 3TA, UK.
  • 2 Leicester Institute of Structural and Chemical Biology and Department of Chemistry, University of Leicester, Lancaster Road, Leicester, LE1 7RH, UK.
  • 3 The Department of Chemistry, University of Oxford, Mansfield Road, Oxford, OX1 3TA, UK. christopher.schofield@chem.ox.ac.uk.
  • 4 Stanford University School of Medicine, Department of Molecular and Cellular Physiology, Clark Center, Stanford, CA, 94305-5345, USA. rashed.chowdhury@stanford.edu.

摘要

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.

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