Feb 6, 2014

Asparagine hydroxylation is likely to be a reversible post-translational modification

BioRxiv : the Preprint Server for Biology
Rodrick WallaceAlex von Kriegsheim

Abstract

Amino acid hydroxylation is a common post-translational modification, which generally regulates protein interactions or adds a functional group that can be further modified. Such hydroxylation is currently considered irreversible, necessitating the degradation and re-synthesis of the entire protein to reset the modification. Here we present evidence that the cellular machinery can reverse FIH-mediated asparagine hydroxylation on intact proteins. These data suggest that asparagine hydroxylation is a flexible and dynamic post-translational modification akin to modifications involved in regulating signalling networks, such as phosphorylation, methylation and ubiquitylation.

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Mentioned in this Paper

Metabolic Process, Cellular
Entire Foramen Singulare
Oxygen Metabolic Process
Embedding
Analysis
Muscle Strength
Metabolism
Genetic Code

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