Evidence map›Paper›PMID 15661844›Full record

ArticleRNA (New York, N.Y.)2005

Interaction of RRF and EF-G from E. coli and T. thermophilus with ribosomes from both origins--insight into the mechanism of the ribosome recycling step.

V Samuel Raj, Hideko Kaji, Akira Kaji

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Novel tigecycline resistance mechanisms inEmerging microbes & infections · 2021
    Article
  3. Differential Contribution of Protein Factors and 70S Ribosome to Elongation.International journal of molecular sciences · 2021
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
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

3 authors at 2 institutions in 1 country.

V Samuel RajDepartment of Microbiology, School of Medicine, University of Pennsylvania, Room 203B, Johnson Pavilion, 3610 Hamilton Walk, Philadelphia, PA 19104, USA.
Hideko Kaji
Akira Kaji
Thomas Jefferson University · USBiomedical Research Institute · US

Funding

RIBOSOME RECYCLING FACTOR(RRF) IN PROKARYOTESR01GM060429 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI KAJI, AKIRA · 2001 to 2004
$1.1M
NIGMS NIH HHS GM 60429NIGMS NIH HHS R01 GM060429
6 · The paper itself

Abstract

Ribosome recycling factor (RRF), elongation factor-G (EF-G), and ribosomes from Thermus thermophilus (tt-) and Escherichia coli (ec-) were used to study the disassembly mechanism of post-termination ribosomal complexes by these factors. With tt-RRF, ec-EF-G can release bound-tRNA from ec-model post-termination complexes. However, tt-RRF is not released by ec-EF-G from ec-ribosomes. This complex with tt-RRF and ec-ribosomes after the tRNA release by ec-EF-G is regarded as an intermediate of the disassembly reaction. Not only tt-RRF, but also mRNA, cannot be released from ec-ribosomes by tt-RRF and ec-EF-G. These data suggest that the release of RRF from ribosomes is coupled or closely related to the release of mRNA during disassembly of post-termination complexes. With tt-ribosomes, ec-EF-G cannot release ribosome-bound ec-RRF even though they are from the same species, showing that proper interaction of ec-RRF and ec-EF-G does not occur on tt-ribosomes. On the other hand, in contrast to a published report, tt-EF-G functions with ec-RRF to disassemble ec-post-termination complexes. In support of this finding, tt-EF-G translocates peptidyl tRNA on ec-ribosomes and catalyzes ec-ribosome-dependent GTPase, showing that tt-EF-G has in vitro translocation activity with ec-ribosomes. Since tt-EF-G with ec-RRF can release tRNA from ec-post-termination complexes, the data are consistent with the hypothesis that the release of tRNA by RRF and EF-G from post-termination complexes is a result of a translocation-like activity of EF-G on RRF.

Indexed as

Base SequenceCatalysisDNA PrimersEscherichia coliGuanosine TriphosphateHydrolysisPeptide Elongation Factor GProtein BindingProteinsRibosomal ProteinsRibosomesThermus thermophilusDNA PrimersGuanosine TriphosphatePeptide Elongation Factor GProteinsRibosomal Proteinsribosome releasing factor

Identifiers

PMID15661844
PMCPMC1370717
OpenAlexW2170812772

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.