Role of a Peptide Tagging System in Degradation of Proteins Synthesized from Damaged Messenger RNA

@article{Keiler1996RoleOA,
  title={Role of a Peptide Tagging System in Degradation of Proteins Synthesized from Damaged Messenger RNA},
  author={Kenneth C. Keiler and Patrick R. H. Waller and Robert T. Sauer},
  journal={Science},
  year={1996},
  volume={271},
  pages={990 - 993}
}
Variants of λ repressor and cytochrome b562 translated from messenger RNAs without stop codons were modified by carboxyl terminal addition of an ssrA-encoded peptide tag and subsequently degraded by carboxyl terminal-specific proteases present in both the cytoplasm and periplasm of Escherichia coli. The tag appears to be added to the carboxyl terminus of the nascent polypeptide chain by cotranslational switching of the ribosome from the damaged messenger RNA to ssrA RNA. 
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    Proceedings of the National Academy of Sciences of the United States of America
  • 2001
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The structural, functional and phylogenetic properties of this unique RNA and its associated factors are reviewed, and the intracellular proteases that act to degrade the proteins tagged by this system are also discussed.
Bacterial SsrA system plays a role in coping with unwanted translational readthrough caused by suppressor tRNAs
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The aim of the present study is to examine how translational readthrough by suppressor tRNAs affects trans‐translation in Escherichia coli.
Analysis of the Role of trans-Translation in the Requirement of tmRNA for l imm P 22 Growth in Escherichia coli
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Quality control of the elongation step of protein synthesis by tmRNP.
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Trans-translation is a quality-control process, activated upon premature termination of protein elongation, which recycles stalled ribosomes and degrades incomplete polypeptides through transfer-messenger RNA, a small stable RNA molecule encoded by the SsrA gene found in bacteria, chloroplasts and mitochondria.
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    Proceedings of the National Academy of Sciences of the United States of America
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TLDR
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