Abstract
Pupylation is a reversible process in which the prokaryotic ubiquitin-like protein Pup is attached to target proteins by an isopeptide bond. It occurs mainly in Actinobacteria and was discovered in Mycobacterium tuberculosis, where pupylated proteins are targeted for proteasomal degradation, thus resembling ubiquitination in eukaryotes. Interestingly, species without a proteasome like Corynebacterium glutamicum also perform pupylation. Key features of this protein modification are summarized here.
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