Journal
MEDCHEMCOMM
Volume 3, Issue 1, Pages 80-85Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c1md00225b
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Funding
- DFG [BO1748-3]
- Biotechnology and Biological Sciences Research Council
- European Union
- Wellcome Trust
- Glasstone Fellowship
- Biotechnology and Biological Sciences Research Council [BB/D011523/1] Funding Source: researchfish
- BBSRC [BB/D011523/1] Funding Source: UKRI
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The lysyl 5S-hydroxylase, JMJD6 acts on proteins involved in RNA splicing. We find that in the absence of substrate JMJD6 catalyses turnover of 2OG to succinate. H-1-NMR analyses demonstrate that consumption of 2OG is coupled to succinate formation. MS analyses reveal that JMJD6 undergoes self-hydroxylation in the presence of Fe(II) and 200 resulting in production of 5S-hydroxylysine residues. JMJD6 in human cells is also found to be hydroxylated. Self-hydroxylation of JMJD6 may play a regulatory role in modulating the hydroxylation status of proteins involved in RNA splicing.
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