Evidence map›Paper›PMID 24808175›Full record

ArticleThe Journal of biological chemistry2014

Signal recognition particle-ribosome binding is sensitive to nascent chain length.

Thomas R Noriega, Albert Tsai, Margaret M Elvekrog, Alexey Petrov, Saskia B Neher, Jin Chen, Niels Bradshaw, Joseph D Puglisi, Peter Walter

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

33 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
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  8. Spatiotemporal kinetics of the SRP pathway in liveProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Article
  10. Review
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  14. Article
  15. Translational Control of Secretory Proteins in Health and Disease.International journal of molecular sciences · 2020
    Review
  16. Review
  17. Improved activity and expression of recombinant human factor IX by propeptide engineering.Daru : journal of Faculty of Pharmacy, Tehran University of Medical Sciences · 2019
    Article
  18. Article
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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

9 authors at 3 institutions in 1 country.

Thomas R NoriegaFrom the Howard Hughes Medical Institute, Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, California 94158.
Albert Tsaithe Department of Structural Biology, Stanford University School of Medicine, Stanford, California 94305, and the Department of Applied Physics, Stanford University, Stanford, California 94305.
Margaret M ElvekrogFrom the Howard Hughes Medical Institute, Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, California 94158.
Alexey Petrovthe Department of Structural Biology, Stanford University School of Medicine, Stanford, California 94305, and.
Saskia B NeherFrom the Howard Hughes Medical Institute, Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, California 94158.
Jin Chenthe Department of Structural Biology, Stanford University School of Medicine, Stanford, California 94305, and the Department of Applied Physics, Stanford University, Stanford, California 94305.
Niels BradshawFrom the Howard Hughes Medical Institute, Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, California 94158.
Joseph D Puglisithe Department of Structural Biology, Stanford University School of Medicine, Stanford, California 94305, and puglisi@stanford.edu.
Peter WalterFrom the Howard Hughes Medical Institute, Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, California 94158, peter@walterlab.ucsf.edu.
Howard Hughes Medical Institute · USStanford University · USUniversity of California, San Francisco · US

Funding

GENETICS OF EUCARYOTIC AND PROCARYOTIC ORGANISMST32GM007810 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ASHRAFI, KAVEH, NARLIKAR, GEETA J · 1985 to 2020
$15.1M
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
Howard Hughes Medical InstituteNIGMS NIH HHS GM032384NIGMS NIH HHS GM099687NIGMS NIH HHS GM51266NIGMS NIH HHS R01 GM032384NIGMS NIH HHS R01 GM051266NIGMS NIH HHS R01 GM099687NIGMS NIH HHS R37 GM032384NIGMS NIH HHS T32 GM007810
6 · The paper itself

Abstract

The signal recognition particle (SRP) directs ribosome-nascent chain complexes (RNCs) displaying signal sequences to protein translocation channels in the plasma membrane of prokaryotes and endoplasmic reticulum of eukaryotes. It was initially proposed that SRP binds the signal sequence when it emerges from an RNC and that successful binding becomes impaired as translation extends the nascent chain, moving the signal sequence away from SRP on the ribosomal surface. Later studies drew this simple model into question, proposing that SRP binding is unaffected by nascent chain length. Here, we reinvestigate this issue using two novel and independent fluorescence resonance energy transfer assays. We show that the arrival and dissociation rates of SRP binding to RNCs vary according to nascent chain length, resulting in the highest affinity shortly after a functional signal sequence emerges from the ribosome. Moreover, we show that SRP binds RNCs in multiple and interconverting conformations, and that conversely, RNCs exist in two conformations distinguished by SRP interaction kinetics.

Indexed as

Models, BiologicalEscherichia coliProtein BiosynthesisRibosomesSignal Recognition ParticleSignal Recognition ParticleFluorescence Resonance Energy Transfer (FRET)Protein TargetingRibosome FunctionSignal Recognition Particle (SRP)Single-Molecule Biophysics

Identifiers

PMID24808175
PMCPMC4094042
OpenAlexW2063908859

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.