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The pupylation pathway and its role in mycobacteria
Jonas Barandun1, Cyrille L Delley, Eilika Weber-Ban
1ETH Zurich, Institute of Molecular Biology & Biophysics, CH-8093 Zurich, Switzerland.
BMC Biology
|December 4, 2012
Summary
Pupylation, a protein modification in actinobacteria, attaches prokaryotic ubiquitin-like protein (Pup) to target proteins for degradation. This pathway is crucial for Mycobacterium tuberculosis survival within hosts.
Area of Science:
- Biochemistry
- Molecular Biology
- Microbiology
Background:
- Pupylation is a post-translational modification in actinobacteria.
- It involves conjugating prokaryotic ubiquitin-like protein (Pup) to target proteins.
- This process targets proteins for proteasomal degradation.
Purpose of the Study:
- To compare the mechanism of Pup-conjugation with ubiquitination.
- To describe the evolutionary emergence of the pupylation pathway.
- To discuss the role of pupylation in Mycobacterium tuberculosis host survival.
Main Methods:
- Comparative analysis of pupylation and ubiquitination mechanisms.
- Evolutionary analysis of pupylation enzymes.
- Functional studies on Mycobacterium tuberculosis survival.
Main Results:
- Pupylation mechanism differs from ubiquitination despite functional similarity.
- Pupylation enzymes evolved from bacterial carboxylate-amine ligases.
- The pupylation pathway is essential for Mycobacterium tuberculosis pathogenesis.
Conclusions:
- Pupylation is a distinct and vital post-translational modification system.
- Understanding pupylation offers insights into bacterial survival strategies.
- This pathway represents a potential target for novel therapeutics.
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