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. 
When Proteins Receive Deadly Messages at Birth
TLDR
A new prokaryotic protein tagging system reported by Keiler et al. involves nascent polypeptides, translated from truncated mRNAs lacking stop codons, receiving short COOH-terminal peptide tags encoded by a separate RNA, 10Sa RNA.
Proteolytic Adaptor for Transfer-Messenger RNA-Tagged Proteins from α-Proteobacteria
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An analog of SspB, the proteolytic adaptor for transfer-messenger RNA (tmRNA)-tagged proteins, in Caulobacter crescentus is identified and is required for optimal proteolysis of tagged proteins in vivo.
The fate of extracellular proteins tagged by the SsrA system of Bacillus subtilis.
TLDR
The polarity of the C-terminus of heterologous hIL-3 protein proved to be an important determinant for protein stability when produced by B. subtilis and it appears that intracellular proteins are the predominant natural substrates of SsrA.
Protein factors associated with the SsrA⋅SmpB tagging and ribosome rescue complex
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  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 2001
TLDR
Evidence is presented here for the existence of a larger ribonucleoprotein complex that contains ribosomal protein S1, phosphoribosyl pyrophosphate synthase, RNase R, and YfbG in addition to SsrA RNA and SmpB.
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TLDR
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
TLDR
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
The small, stable RNA molecule encoded by ssrA, known as tmRNA or 10Sa RNA, is required for the growth of certain hybrid limm phages in Escherichia coli. tmRNA has been shown to tag partially
Lon Protease Degrades Transfer-Messenger RNA-Tagged Proteins
TLDR
In vivo and in vitro evidence is presented that demonstrates a direct role for the Lon ATP-dependent protease in the degradation of tmRNA-tagged proteins, and highly purified Lon preferentially degraded the tm RNA-taged forms of proteins compared to the untagged forms.
A specificity-enhancing factor for the ClpXP degradation machine.
TLDR
Here, a ribosome-associated protein, SspB, was found to bind specifically to ssrA-tagged proteins and to enhance recognition of these proteins by ClpXP, demonstrating that SSPB is a specificity-enhancing factor for Clp XP that controls substrate choice.
Quality control of the elongation step of protein synthesis by tmRNP.
TLDR
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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