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Bacterial Expression and Purification of Human Matrix Metalloproteinase-3 using Affinity Chromatography
Published on: March 30, 2022
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JMJD5 is a human arginyl C-3 hydroxylase.
Sarah E Wilkins1, Md Saiful Islam1, Joan M Gannon1
1The Department of Chemistry, University of Oxford, Mansfield Road, Oxford, OX1 3TA, UK.
Nature Communications
|March 23, 2018
Summary
Jumonji-C domain-containing protein 5 (JMJD5) is identified as an arginine hydroxylase, not a lysine demethylase. This finding reveals JMJD5
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- Oxygenase-catalyzed post-translational modifications are crucial for cellular functions.
- Jumonji-C (JmjC) domain-containing protein 5 (JMJD5) is essential for animal development and previously identified as a histone Nε-methyl lysine demethylase (KDM).
Purpose of the Study:
- To investigate the enzymatic activity of JMJD5.
- To clarify the role of JMJD5 in protein modification.
Main Methods:
- Extensive peptide screening based on JMJD5 interacting proteins.
- High-resolution crystallographic analyses.
Main Results:
- JMJD5 catalyzes the stereoselective C-3 hydroxylation of arginine residues in specific protein sequences (RCCD1 and RPS6).
- Crystallographic data support JMJD5's function as an arginine hydroxylase, contradicting its prior classification as a KDM.
Conclusions:
- JMJD5 functions as an arginine hydroxylase, not a lysine demethylase.
- Understanding JMJD5's enzymatic activity is vital for developing targeted therapies for cancer and genetic diseases.
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