Evidence map›Paper›PMID 24836001›Full record

ArticleCell reports2014

The dynamics of SecM-induced translational stalling.

Albert Tsai, Guy Kornberg, Magnus Johansson, Jin Chen, Joseph D Puglisi

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

28 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Partial spontaneous intersubunit rotations in pretranslocation ribosomes.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Nature and Regulation of Protein Folding on the Ribosome.Trends in biochemical sciences · 2019
    Review
  14. Ribosome collisions alter frameshifting at translational reprogramming motifs in bacterial mRNAs.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. The ribosome and its role in protein folding: looking through a magnifying glass.Acta crystallographica. Section D, Structural biology · 2017
    Review
  20. Amino acid sequence repertoire of the bacterial proteome and the occurrence of untranslatable sequences.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
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

5 authors at 1 institution in 1 country.

Albert TsaiDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305-5126, USA; Department of Applied Physics, Stanford University, Stanford, CA 94305-4090, USA.
Guy KornbergDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305-5126, USA.
Magnus JohanssonDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305-5126, USA.
Jin ChenDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305-5126, USA; Department of Applied Physics, Stanford University, Stanford, CA 94305-4090, USA.
Joseph D PuglisiDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305-5126, USA; Stanford Magnetic Resonance Laboratory, Stanford University School of Medicine, Stanford, CA 94305-5126, USA. Electronic address: puglisi@stanford.edu.
Stanford University · US

Funding

STRUCTURAL BASIS FOR RIBOSOME FUNCTIONSR01GM051266 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI PUGLISI, JOSEPH D · 1995 to 2021
$7.7M
Molecular Biophysics Training Program at StanfordT32GM008294 · NIGMS · STANFORD UNIVERSITY · PI HUANG, KERWYN C. · 1989 to 2019
$7.4M
Single molecule translational profilingR01GM099687 · NIGMS · STANFORD UNIVERSITY · PI PUGLISI, JOSEPH D · 2011 to 2015
$4.3M
NIGMS NIH HHS GM099687NIGMS NIH HHS GM51266NIGMS NIH HHS R01 GM051266NIGMS NIH HHS R01 GM099687NIGMS NIH HHS T32 GM008294
6 · The paper itself

Abstract

SecM is an E. coli secretion monitor capable of stalling translation on the prokaryotic ribosome without cofactors. Biochemical and structural studies have demonstrated that the SecM nascent chain interacts with the 50S subunit exit tunnel to inhibit peptide bond formation. However, the timescales and pathways of stalling on an mRNA remain undefined. To provide a dynamic mechanism for stalling, we directly tracked the dynamics of elongation on ribosomes translating the SecM stall sequence (FSTPVWISQAQGIRAGP) using single-molecule fluorescence techniques. Within 1 min, three peptide-ribosome interactions work cooperatively over the last five codons of the SecM sequence, leading to severely impaired elongation rates beginning from the terminal proline and lasting four codons. Our results suggest that stalling is tightly linked to the dynamics of elongation and underscore the roles that the exit tunnel and nascent chain play in controlling fundamental steps in translation.

Indexed as

Peptide Chain Elongation, TranslationalAmino Acid SequenceCodonEscherichia coliEscherichia coli ProteinsMolecular Sequence DataRibosomesTranscription FactorsCodonEscherichia coli ProteinsSecM protein, E coliTranscription Factors

Identifiers

PMID24836001
PMCPMC4059775
OpenAlexW2022567074

What OpenQuestion holds

Textmetadata
LicenceTDM
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.