Evidence map›Paper›PMID 11891313›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

Stop codons preceded by rare arginine codons are efficient determinants of SsrA tagging in Escherichia coli.

Christopher S Hayes, Baundauna Bose, Robert T Sauer

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
3.5field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

61 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Translation efficiency is maintained at elevated temperature inThe Journal of biological chemistry · 2018
    Article
  6. Article
  7. Mechanisms of ribosome rescue in bacteria.Nature reviews. Microbiology · 2015
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Engineering genes for predictable protein expression.Protein expression and purification · 2012
    Review
  20. The tmRNA ribosome-rescue system.Advances in protein chemistry and structural biology · 2012
    Review

1 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Christopher S HayesDepartment of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
Baundauna Bose
Robert T Sauer
Massachusetts Institute of Technology · US

Funding

REPRESSOR &ANTIREPRESSOR PROTEINS OF BACTERIOPHAGER01AI016892 · NIAID · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BAKER, TANIA A, SAUER, ROBERT T · 1985 to 2022
$13.0M
NIAID NIH HHS AI-16892NIAID NIH HHS R01 AI016892
6 · The paper itself

Abstract

The SsrA or tmRNA quality control system intervenes when ribosomes stall on mRNAs and directs the addition of a C-terminal peptide tag that targets the modified polypeptide for degradation. Although hundreds of SsrA-tagged proteins can be detected in cells when degradation is prevented, most of these species have not been identified. Consequently, the mRNA sequence determinants that cause ribosome stalling and SsrA tagging are poorly understood. SsrA tagging of Escherichia coli ribokinase occurs at three specific sites at or near the C terminus of this protein. The sites of tagging correspond to ribosome stalling at the termination codon and at rare AGG codons encoding Arg-307 and Arg-309, the antepenultimate and C-terminal residues of E. coli ribokinase. Mutational analyses and studies of the effects of overexpressing the tRNA that decodes AGG reveal that the combination of a rare arginine codon at the C terminus and the adjacent inefficient UGA termination codon act to recruit the SsrA-tagging system, presumably by slowing the rate of translation elongation and termination.

Indexed as

Amino Acid SequenceArginineBase SequenceCodon, TerminatorEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialGenes, BacterialMolecular Sequence DataMutationPhosphotransferases (Alcohol Group Acceptor)Protein BiosynthesisProtein Processing, Post-TranslationalRegulatory Sequences, Nucleic AcidRibosomesRNA, BacterialArginineCodon, TerminatorEscherichia coli ProteinsPhosphotransferases (Alcohol Group Acceptor)ribokinaseRNA, BacterialRNA, Transfer, ArgtmRNA

Identifiers

PMID11891313
PMCPMC122542
OpenAlexW2012573942

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.