Evidence map›Paper›PMID 25358118›Full record

ArticleeLife2014

Real-time observation of signal recognition particle binding to actively translating ribosomes.

Thomas R Noriega, Jin Chen, Peter Walter, Joseph D Puglisi

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
5.1field-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

30 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Spatiotemporal kinetics of the SRP pathway in liveProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. Article
  7. Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Dynamics of translation can determine the spatial organization of membrane-bound proteins and their mRNA.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

4 authors at 2 institutions in 1 country.

Thomas R NoriegaHoward Hughes Medical Institute, University of California, San Francisco, San Francisco, United States.
Jin ChenDepartment of Structural Biology, Stanford University School of Medicine, Stanford, United States.ORCID http://orcid.org/0000-0002-6634-4397
Peter WalterHoward Hughes Medical Institute, University of California, San Francisco, San Francisco, United States.
Joseph D PuglisiDepartment of Structural Biology, Stanford University School of Medicine, Stanford, United States.
Howard Hughes Medical Institute · USStanford University · US

Funding

STRUCTURAL BASIS FOR RIBOSOME FUNCTIONSR01GM051266 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI PUGLISI, JOSEPH D · 1995 to 2021
$7.7M
MECHANISM OF PROTEIN TRANSLOCATION ACROSS MEMBRANESR01GM032384 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 1985 to 2023
$7.6M
Single molecule translational profilingR01GM099687 · NIGMS · STANFORD UNIVERSITY · PI PUGLISI, JOSEPH D · 2011 to 2015
$4.3M
MECHANISM OF PROTEIN TRANSLOCATION ACROSS MEMBRANESR37GM032384 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI WALTER, PETER · 1993 to 2002
$907k
NIGMS NIH HHS GM032384NIGMS NIH HHS GM099687NIGMS NIH HHS GM51266NIGMS NIH HHS R01 GM032384NIGMS NIH HHS R01 GM051266NIGMS NIH HHS R01 GM099687NIGMS NIH HHS R37 GM032384
6 · The paper itself

Abstract

The signal recognition particle (SRP) directs translating ribosome-nascent chain complexes (RNCs) that display a signal sequence to protein translocation channels in target membranes. All previous work on the initial step of the targeting reaction, when SRP binds to RNCs, used stalled and non-translating RNCs. This meant that an important dimension of the co-translational process remained unstudied. We apply single-molecule fluorescence measurements to observe directly and in real-time E. coli SRP binding to actively translating RNCs. We show at physiologically relevant SRP concentrations that SRP-RNC association and dissociation rates depend on nascent chain length and the exposure of a functional signal sequence outside the ribosome. Our results resolve a long-standing question: how can a limited, sub-stoichiometric pool of cellular SRP effectively distinguish RNCs displaying a signal sequence from those that are not? The answer is strikingly simple: as originally proposed, SRP only stably engages translating RNCs exposing a functional signal sequence.

Indexed as

Computer SystemsProtein BiosynthesisCalibrationEscherichia coliEscherichia coli ProteinsKineticsPeptide Chain Initiation, TranslationalProtein BindingRibosomesSignal Recognition ParticleEscherichia coli ProteinsSignal Recognition Particlebiophysicscell biologyE. coliprotein targetingribosome translationsignal recognition particlesingle molecule fluorescencestructural biology

Identifiers

PMID25358118
PMCPMC4213662
OpenAlexW2156470254

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.