This title appears in the Scientific Report : 2014 

Pupylated proteins in Corynebacterium glutamicum revealed by MudPIT analysis
Küberl, Andreas (Corresponding Author)
Fränzel, Benjamin / Eggeling, Lothar / Polen, Tino / Wolters, Dirk Andreas / Bott, Michael
Biotechnologie; IBG-1
Proteomics, 14 (2014) 12, S. 1531 - 1542
Weinheim Wiley VCH 2014
Journal Article
ohne Topic
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In amanner similar to ubiquitin, the prokaryotic ubiquitin-like protein (Pup) has been shown totarget proteins for degradation via the proteasome inmycobacteria. However, not all actinobacteriapossessing the Pup protein also contain a proteasome. In this study, we set out to studypupylation in the proteasome-lacking non-pathogenic model organism Corynebacterium glutamicum.A defined pup deletion mutant of C. glutamicum ATCC 13032 grew aerobically as theparent strain in standard glucose minimal medium, indicating that pupylation is dispensableunder these conditions. After expression of a Pup derivative carrying an aminoterminal polyhistidinetag in the pup mutant and Ni2+-chelate affinity chromatography, pupylated proteinswere isolated. Multidimensional protein identification technology (MudPIT) andMALDI-TOFMS/MS of the elution fraction unraveled 55 proteins being pupylated in C. glutamicum and 66pupylation sites. Similar to mycobacteria, the majority of pupylated proteins are involved inmetabolism or translation. Our results define the first pupylome of an actinobacterial specieslacking a proteasome, confirming that other fates besides proteasomal degradation are possiblefor pupylated proteins.