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Access to the article is free, however registration and sign-in are required.Tuberculosis, a devastating infectious disease caused by Mycobacterium tuberculosis (Mtb), is a global health threat that presently afflicts one-third of the world's population. The culprit bacterium is an obligate and persistent pathogen that maintains viability, in a latent state, within phagocytes--cells that ingest foreign materials and microorganisms--that reside in the lungs of humans. Treating tuberculosis requires prolonged antibiotic therapy that can result in multidrug-resistant Mtb strains. Because the bacterium is highly infectious, grows extremely slowly, and is difficult to manipulate genetically, the discovery of new drugs to combat Mtb infection is challenging. Thus, identifying Mtb components as potential drug targets is one of the key approaches to developing new tuberculosis therapy. Pearce et al. report the discovery of a protein (Pup) in Mtb that modifies other bacterial proteins to target them for degradation. The process is similar to that in eukaryotes, in which the protein ubiquitin modifies proteins and targets them for proteolysis. The discovery of this process in prokaryotes opens the door to further characterizing a protein regulatory mechanism that could be targeted by pathogen-specific drugs.

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      Keywords:

      NSDL,NSDL_SetSpec_BEN,Mycobacterium tuberculosis (Mtb),posttranslational protein modification,protein degradation complex,proteasome accessory factor A,Mycobacterium proteasomal adenosine triphosphatase (ATPase),Tuberculosis,Life Science,proteolysis,ubiquitin,Pup,oai:nsdl.org:2200/20110722030522494T

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      English

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