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The pupylation pathway and its role in mycobacteria

Jonas Barandun, Cyrille L Delley and Eilika Weber-Ban*

Author Affiliations

ETH Zurich, Institute of Molecular Biology & Biophysics, CH-8093 Zurich, Switzerland

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BMC Biology 2012, 10:95  doi:10.1186/1741-7007-10-95

Published: 30 November 2012

Abstract

Pupylation is a post-translational protein modification occurring in actinobacteria through which the small, intrinsically disordered protein Pup (prokaryotic ubiquitin-like protein) is conjugated to lysine residues of proteins, marking them for proteasomal degradation. Although functionally related to ubiquitination, pupylation is carried out by different enzymes that are evolutionarily linked to bacterial carboxylate-amine ligases. Here, we compare the mechanism of Pup-conjugation to target proteins with ubiquitination, describe the evolutionary emergence of pupylation and discuss the importance of this pathway for survival of Mycobacterium tuberculosis in the host.