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Originally published in Science Express on 2 October 2008
Science 14 November 2008:
Vol. 322. no. 5904, pp. 1104 - 1107
DOI: 10.1126/science.1163885
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Reports

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 Darwin1*

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.

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

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

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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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