Ubiquitin-Like Protein Involved in the Proteasome Pathway of Mycobacterium tuberculosis
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- 14 November 2008
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 322 (5904) , 1104-1107
- https://doi.org/10.1126/science.1163885
Abstract
The protein modifier ubiquitin is a signal for proteasome-mediated degradation in eukaryotes. Proteasome-bearing prokaryotes have been thought to degrade proteins via a ubiquitin-independent pathway. We have identified a prokaryotic ubiquitin-like protein, Pup (Rv2111c), which was specifically conjugated to proteasome substrates in the pathogen Mycobacterium tuberculosis. Pupylation occurred on lysines and required proteasome accessory factor A (PafA). In a pafA mutant, pupylated proteins were absent and substrates accumulated, thereby connecting pupylation with degradation. Although analogous to ubiquitylation, pupylation appears to proceed by a different chemistry. Thus, like eukaryotes, bacteria may use a small-protein modifier to control protein stability.Keywords
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