Evidence map›Paper›PMID 15534366›Full record

ArticleNucleic acids research2004

Testing the conservation of the translational machinery over evolution in diverse environments: assaying Thermus thermophilus ribosomes and initiation factors in a coupled transcription-translation system from Escherichia coli.

Jill Thompson, Albert E Dahlberg

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2004. 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
0.5field-weighted citation impact, top 39% 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, 25 citations in OpenAlex.

  1. Article
  2. 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. Structure of the protein core of translation initiation factor 2 in apo, GTP-bound and GDP-bound forms.Acta crystallographica. Section D, Biological crystallography · 2013
    Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  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

2 authors at 1 institution in 1 country.

Jill ThompsonDepartment of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI 02912, USA. Jill_Rosemary_Thompson@brown.edu
Albert E Dahlberg
Brown University · US

Funding

POLYSOMES &SUBUNITS: STRUCTURE-FUNCTION RELATIONSHIPSR01GM019756 · NIGMS · BROWN UNIVERSITY · PI DAHLBERG, ALBERT E · 1985 to 2013
$8.5M
INDENTATION WITH ATOMIC FORCE MICROSCOPYF32GM019756 · NIGMS · BARNES-JEWISH HOSPITAL · PI COSTA, KEVIN D · 1998 to 1998
–
NIGMS NIH HHS F32 GM019756NIGMS NIH HHS GM19756NIGMS NIH HHS R01 GM019756
6 · The paper itself

Abstract

Ribosomes from the extreme thermophile Thermus thermophilus are capable of translation in a coupled transcription-translation system derived from Escherichia coli. At 45 degrees C, T.thermophilus ribosomes translate at approximately 25-30% of the maximal rate of E.coli ribosomes, and synthesize full-length protein. T.thermophilus and E.coli subunits can be combined to effect translation, with the spectrum of proteins produced depending upon the source of the 30S subunit. In this system, T.thermophilus ribosomes function in concert with E.coli translational factors and tRNAs, with elongation and release factors being supplied from the E.coli extract, and purified initiation factors (IFs) being added exogenously. Cloned and purified T.thermophilus IF1, IF2 and IF3 supported the synthesis of the same products in vitro as the E.coli factors, although the relative levels of some polypeptides were factor dependent. We conclude that, at least between these two phylogenetically distant species, translational factor function and subunit-subunit interactions are conserved. This functional compatibility is remarkable given the extreme and highly divergent environments to which these species have adapted.

Indexed as

Protein BiosynthesisTranscription, GeneticEscherichia coliEvolution, MolecularPeptide Initiation FactorsRibosomesTemperatureThermus thermophilusPeptide Initiation Factors

Identifiers

PMID15534366
PMCPMC528807
OpenAlexW2007345851

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.