Evidence map›Paper›PMID 22853911›Full record

ArticleBiophysical journal2012

Mechanisms of SecM-mediated stalling in the ribosome.

James Gumbart, Eduard Schreiner, Daniel N Wilson, Roland Beckmann, Klaus Schulten

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

45 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
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  9. Common sequence motifs of nascent chains engage the ribosome surface and trigger factor.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Forcing the ribosome to change its message.The Journal of biological chemistry · 2020
    Article
  15. Article
  16. Article
  17. Article
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  20. Review
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 3 institutions in 2 countries.

James GumbartBiosciences Division, Argonne National Laboratory, Argonne, Illinois, USA.
Eduard Schreiner
Daniel N Wilson
Roland Beckmann
Klaus Schulten
Center for Integrated Protein Science Munich · DEUniversity of Illinois Urbana-Champaign · USArgonne National Laboratory · US

Funding

WHOLE CELL SIMULATIONP41RR005969 · NCRR · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI STONE, JOHN H · 1990 to 2011
$19.8M
System-Level Simulation of a Bioenergetic MembraneR01GM067887 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2003 to 2018
$4.0M
NCRR NIH HHS P41 RR005969NIGMS NIH HHS R01 GM067887
6 · The paper itself

Abstract

Nascent-peptide modulation of translation is a common regulatory mechanism of gene expression. In this mechanism, while the nascent peptide is still in the exit tunnel of the ribosome, it induces translational pausing, thereby controlling the expression of downstream genes. One example is SecM, which inhibits peptide-bond formation in the ribosome's peptidyl transferase center (PTC) during its own translation, upregulating the expression of the protein translocase SecA. Although biochemical experiments and cryo-electron microscopy data have led to the identification of some residues involved in SecM recognition, the full pathway of interacting residues that connect SecM to the PTC through the ribosome has not yet been conclusively established. Here, using the cryo-electron microscopy data, we derived the first (to our knowledge) atomic model of the SecM-stalled ribosome via molecular-dynamics flexible fitting, complete with P- and A-site tRNAs. Subsequently, we carried out simulations of native and mutated SecM-stalled ribosomes to investigate possible interaction pathways between a critical SecM residue, R163, and the PTC. In particular, the simulations reveal the role of SecM in altering the position of the tRNAs in the ribosome, and thus demonstrate how the presence of SecM in the exit tunnel induces stalling. Finally, steered molecular-dynamics simulations in which SecM was pulled toward the tunnel exit suggest how SecA interacting with SecM from outside the ribosome relieves stalling.

Indexed as

Protein BiosynthesisAdenosine TriphosphatasesAmino AcidsBacterial ProteinsComputational BiologyEscherichia coliEscherichia coli ProteinsMembrane Transport ProteinsModels, MolecularMutationPeptidyl TransferasesPliabilityProtein BindingProtein ConformationRibosomesSecA ProteinsAdenosine TriphosphatasesAmino AcidsBacterial ProteinsEscherichia coli ProteinsMembrane Transport ProteinsPeptidyl TransferasesSecA ProteinsSecM protein, E coliSEC Translocation ChannelsTranscription Factors

Identifiers

PMID22853911
PMCPMC3400775
OpenAlexW2030359164

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.