Evidence map›Paper›PMID 15509870›Full record

ArticleNucleic acids research2004

Multiple defects in translation associated with altered ribosomal protein L4.

Michael O'Connor, Steven T Gregory, 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 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.8field-weighted citation impact, top 16% 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, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.International journal of molecular sciences · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Pseudouridine-Free Escherichia coli Ribosomes.Journal of bacteriology · 2018
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Evolution of molecular error rates and the consequences for evolvability.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Michael O'ConnorSchool of Biological Sciences, University of Missouri-Kansas City, 5007 Rockhill Road, Kansas City, MO 64110, USA. oconnormi@umkc.edu
Steven T Gregory
Albert E Dahlberg
University of Missouri–Kansas City · 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

The ribosomal proteins L4 and L22 form part of the peptide exit tunnel in the large ribosomal subunit. In Escherichia coli, alterations in either of these proteins can confer resistance to the macrolide antibiotic, erythromycin. The structures of the 30S as well as the 50S subunits from each antibiotic resistant mutant differ from wild type in distinct ways and L4 mutant ribosomes have decreased peptide bond-forming activity. Our analyses of the decoding properties of both mutants show that ribosomes carrying the altered L4 protein support increased levels of frameshifting, missense decoding and readthrough of stop codons during the elongation phase of protein synthesis and stimulate utilization of non-AUG codons and mutant initiator tRNAs at initiation. L4 mutant ribosomes are also altered in their interactions with a range of 30S-targeted antibiotics. In contrast, the L22 mutant is relatively unaffected in both decoding activities and antibiotic interactions. These results suggest that mutations in the large subunit protein L4 not only alter the structure of the 50S subunit, but upon subunit association, also affect the structure and function of the 30S subunit.

Indexed as

Protein BiosynthesisCodonCodon, TerminatorErythromycinEscherichia coliFrameshifting, RibosomalMutationMutation, MissenseProtein Synthesis InhibitorsRibosomal ProteinsRibosomesRNA, MessengerRNA, Transfer, MetCodonCodon, TerminatorErythromycinProtein Synthesis Inhibitorsribosomal protein L4Ribosomal ProteinsRNA, MessengerRNA, Transfer, Met

Identifiers

PMID15509870
PMCPMC528798
OpenAlexW2141824716

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.