Evidence map›Paper›PMID 20974854›Full record

ArticleThe Journal of biological chemistry2010

Pentameric organization of the ribosomal stalk accelerates recruitment of ricin a chain to the ribosome for depurination.

Xiao-Ping Li, Przemyslaw Grela, Dawid Krokowski, Marek Tchórzewski, Nilgun E Tumer

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

24 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Biomolecular NMR assignments · 2024
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Potential therapeutic applications of plant toxin-ricin in cancer: challenges and advances.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015
    Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Targeting ricin to the ribosome.Toxicon : official journal of the International Society on Toxinology · 2013
    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 2 institutions in 2 countries.

Xiao-Ping LiDepartment of Plant Biology and Pathology, School of Environmental and Biological Sciences, Rutgers University, New Brunswick, New Jersey 08901-8520, USA.
Przemyslaw Grela
Dawid Krokowski
Marek Tchórzewski
Nilgun E Tumer
Maria Curie-Skłodowska University · PLRutgers, The State University of New Jersey · US

Funding

What makes ricin ToxicR01AI072425 · NIAID · RUTGERS, THE STATE UNIV OF N.J. · PI TUMER, NILGUN E · 2007 to 2021
$5.8M
Interaction of ricin A chain with the ribosomal stalkR03TW008418 · FIC · RUTGERS, THE STATE UNIV OF N.J. · PI TUMER, NILGUN E · 2011 to 2013
$172k
FIC NIH HHS R03 TW008418NIAID NIH HHS AI072425NIAID NIH HHS R01 AI072425
6 · The paper itself

Abstract

Ribosome inactivating proteins (RIPs) depurinate a universally conserved adenine in the α-sarcin/ricin loop (SRL) and inhibit protein synthesis at the translation elongation step. We previously showed that ribosomal stalk is required for depurination of the SRL by ricin toxin A chain (RTA). The interaction between RTA and ribosomes was characterized by a two-step binding model, where the stalk structure could be considered as an important interacting element. Here, using purified yeast ribosomal stalk complexes assembled in vivo, we show a direct interaction between RTA and the isolated stalk complex. Detailed kinetic analysis of these interactions in real time using surface plasmon resonance (SPR) indicated that there is only one type of interaction between RTA and the ribosomal stalk, which represents one of the two binding steps of the interaction with ribosomes. Interactions of RTA with the isolated stalk were relatively insensitive to salt, indicating that nonelectrostatic interactions were dominant. We compared the interaction of RTA with the full pentameric stalk complex containing two pairs of P1/P2 proteins with its interaction with the trimeric stalk complexes containing only one pair of P1/P2 and found that the rate of association of RTA with the pentamer was higher than with either trimer. These results demonstrate that the stalk is the main landing platform for RTA on the ribosome and that pentameric organization of the stalk accelerates recruitment of RTA to the ribosome for depurination. Our results suggest that multiple copies of the stalk proteins might also increase the scavenging ability of the ribosome for the translational GTPases.

Indexed as

DimerizationKineticsModels, StatisticalProtein BindingProtein ConformationProtein Structure, TertiaryPurinesRecombinant ProteinsRibosomesRicinStatic ElectricitySurface Plasmon ResonanceTime FactorsPurinesRecombinant ProteinsRicin

Identifiers

PMID20974854
PMCPMC3009872
OpenAlexW1981355738

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.