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.
Highlights
Pupylation is a post-translational protein modification occurring in actinobacteria through which the small, intrinsically disordered protein penultimate position (Pup) is conjugated to lysine residues of proteins, marking them for proteasomal degradation
The existence of a depupylation activity in actinobacteria [11, 12] and the fact that some members harbor the pupylation gene locus without encoding proteasomal subunits suggest that pupylation might fulfill a broader role in regulation and cellular signaling
An ubiquitin-like modification pathway in bacteria marks proteins for proteasomal degradation Actinobacteria form a large and diverse phylum with many members living in close association with eukaryotic hosts as either pathogens (Mycobacterium spp.) or symbionts [15, 16]
Summary
Posttranslational modifications of proteins expanding nature’s inventory. Englewood, Colo.: Roberts and Company Publishers; 2006. 2. 5. Pearce MJ, Mintseris J, Ferreyra J, Gygi SP, Darwin KH: Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis. 6. Burns KE, Liu WT, Boshoff HI, Dorrestein PC, Barry CE, 3rd: Proteasomal protein degradation in Mycobacteria is dependent upon a prokaryotic ubiquitin-like protein. 8. Ranjan N, Damberger FF, Sutter M, Allain FH, Weber-Ban E: Solution structure and activation mechanism of ubiquitin-like small archaeal modifier proteins. 9. Striebel F, Imkamp F, Sutter M, Steiner M, Mamedov A, Weber-Ban E: Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes. Microbiology and molecular biology reviews : MMBR 2007, 71(3):495548
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