Deletion of dop in Mycobacterium smegmatis abolishes pupylation of protein substrates in vivo.

@article{Imkamp2010DeletionOD,
  title={Deletion of dop in Mycobacterium smegmatis abolishes pupylation of protein substrates in vivo.},
  author={Frank Imkamp and Tobias Rosenberger and Frank Striebel and P M Keller and Beat Amstutz and Peter T. Sander and Eilika Weber-Ban},
  journal={Molecular microbiology},
  year={2010},
  volume={75 3},
  pages={744-54}
}
Proteasome-bearing bacteria make use of a ubiquitin-like modification pathway to target proteins for proteasomal turnover. In a process termed pupylation, proteasomal substrates are covalently modified with the small protein Pup that serves as a degradation signal. Pup is attached to substrate proteins by action of PafA. Prior to its attachment, Pup needs to undergo deamidation at its C-terminal residue, converting glutamine to glutamate. This step is catalysed in vitro by Dop. In order to… CONTINUE READING

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