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Published Online October 2, 2008
Science DOI: 10.1126/science.1163885

Reports

Submitted on July 28, 2008
Accepted on September 16, 2008

Ubiquitin-Like Protein Involved in the Proteasome Pathway of Mycobacterium tuberculosis

Michael J. Pearce 1, Julian Mintseris 2, Jessica Ferreyra 1, Steven P. Gygi 2, K. Heran Darwin 1*

1 New York University School of Medicine, Department of Microbiology, New York, NY 10016, USA.
2 Harvard Medical School, Department of Cell Biology, Boston, MA 02115, USA.

* To whom correspondence should be addressed.
K. Heran Darwin , E-mail: heran.darwin{at}med.nyu.edu

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 (Mtb). 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.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Proteasomal Protein Degradation in Mycobacteria Is Dependent upon a Prokaryotic Ubiquitin-like Protein.
K. E. Burns, W.-T. Liu, H. I. M. Boshoff, P. C. Dorrestein, and C. E. Barry 3rd (2009)
J. Biol. Chem. 284, 3069-3075
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Science. ISSN 0036-8075 (print), 1095-9203 (online)