Evidence map›Paper›PMID 19172744›Full record

ArticleNature structural & molecular biology2008

SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.

Saskia B Neher, Niels Bradshaw, Stephen N Floor, John D Gross, Peter Walter

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.2field-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

26 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Review
  3. Targeting of Proteins for Translocation at the Endoplasmic Reticulum.International journal of molecular sciences · 2022
    Review
  4. Article
  5. Article
  6. Article
  7. Ribosome-SRP-FtsY cotranslational targeting complex in the closed state.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Transient tether between the SRP RNA and SRP receptor ensures efficient cargo delivery during cotranslational protein targeting.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  17. Article
  18. Review
  19. Article
  20. It takes two to tango: regulation of G proteins by dimerization.Nature reviews. Molecular cell biology · 2009
    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 1 institution in 1 country.

Saskia B NeherHoward Hughes Medical Institute, University of California at San Francisco, 600 16th Street, San Francisco, California 94158, USA.
Niels Bradshaw
Stephen N Floor
John D Gross
Peter Walter
University of California, San Francisco · US

Funding

MECHANISM OF PROTEIN TRANSLOCATION ACROSS MEMBRANESR01GM032384 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 1985 to 2023
$7.6M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM032384
6 · The paper itself

Abstract

The interaction of the signal-recognition particle (SRP) with its receptor (SR) mediates co-translational protein targeting to the membrane. SRP and SR interact via their homologous core GTPase domains and N-terminal four-helix bundles (N domains). SRP-SR complex formation is slow unless catalyzed by SRP's essential RNA component. We show that truncation of the first helix of the N domain (helix N1) of both proteins dramatically accelerates their interaction. SRP and SR with helix N1 truncations interact at nearly the RNA-catalyzed rate in the absence of RNA. NMR spectroscopy and analysis of GTPase activity show that helix N1 truncation in SR mimics the conformational switch caused by complex formation. These results demonstrate that the N-terminal helices of SRP and SR are autoinhibitory for complex formation in the absence of SRP RNA, suggesting a mechanism for RNA-mediated coordination of the SRP-SR interaction.

Indexed as

Amino Acid SequenceBacterial ProteinsEscherichia coliEscherichia coli ProteinsGuanosine TriphosphateHydrolysisMacromolecular SubstancesModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein Interaction Domains and MotifsReceptors, Cytoplasmic and NuclearReceptors, PeptideRecombinant ProteinsRNA, Bacterial4.5S RNABacterial ProteinsEscherichia coli ProteinsFfh protein, E coliFtsY protein, BacteriaGuanosine TriphosphateMacromolecular SubstancesReceptors, Cytoplasmic and NuclearReceptors, PeptideRecombinant ProteinsRNA, Bacterialsignal peptide receptorSignal Recognition Particle

Identifiers

PMID19172744
PMCPMC2767265
OpenAlexW2093478556

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.