Unraveling the biochemistry and provenance of pupylation: a prokaryotic analog of ubiquitination
2008
Understanding Pupylation: A Prokaryotic Version of Ubiquitination
publication
Evidence: moderate
Author Information
Author(s): Lakshminarayan Iyer, Maxwell Burroughs, L Aravind
Primary Institution: National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health
Hypothesis
Is PafA the enzyme responsible for the pupylation process in Mycobacterium tuberculosis?
Conclusion
PafA is likely the Pup ligase that catalyzes the ligation of Pup to target proteins in Mycobacterium tuberculosis.
Supporting Evidence
- PafA is predicted to catalyze an ATP-dependent ligation reaction.
- Pup-conjugation is found sporadically outside actinobacteria.
- PafA and Pup are often found in close genomic proximity.
Takeaway
This study shows that a small protein called Pup can attach to other proteins in bacteria, similar to how ubiquitin works in humans, and that a protein named PafA helps this happen.
Methodology
The study used sequence profile searches and comparative genomic analysis to investigate the pupylation process.
Statistical Information
P-Value
10-5
Digital Object Identifier (DOI)
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