Lysyl and prolyl hydroxylations are well-known post-translational modifications to animal and plant proteins with extracellular roles. More recent work has indicated that the hydroxylation of intracellular animal proteins may be common. JMJD6 catalyses the iron- and 2-oxoglutarate-dependent hydroxylation of lysyl residues in arginine-serine-rich domains of RNA-splicing-related proteins. We report crystallographic studies on the catalytic domain of JMJD6 in complex with Ni(II) substituting for Fe(II). Together with mutational studies, the structural data suggest how JMJD6 binds its lysyl residues such that it can catalyse C-5 hydroxylation rather than N(varepsilon)-demethylation, as for analogous enzymes.
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Article Synopsis
- N-acetyl-L-lysine is common in dietary protein, yet its effects on consumers are largely unknown.
- Research indicates that Lysyl-tRNA synthetase (KARS) integrates this compound into proteins during their synthesis, influencing cellular acetylation levels.
- This process, called co-translational modification (coTM), allows for the acetylation of proteins in ways that differ from traditional post-translational modifications, potentially expanding our understanding of protein regulation in cells.
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