Evidence map›Paper›PMID 17198710›Full record

ArticleJournal of molecular biology2007

Importance of the 5 S rRNA-binding ribosomal proteins for cell viability and translation in Escherichia coli.

Alexey P Korepanov, George M Gongadze, Maria B Garber, Donald L Court, Mikhail G Bubunenko

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.0field-weighted citation impact, top 28% 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

22 citing papers in PubMed, 43 citations in OpenAlex.

  1. Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.International journal of molecular sciences · 2024
    Review
  2. Article
  3. Adaptive Responses ofAntimicrobial agents and chemotherapy · 2022
    Article
  4. Article
  5. Simplification of Ribosomes in Bacteria with Tiny Genomes.Molecular biology and evolution · 2021
    Article
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  7. Article
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  17. Article
  18. Inhibition of bacterial ribosome assembly: a suitable drug target?Microbiology and molecular biology reviews : MMBR · 2009
    Review
  19. Ribosome biogenesis and the translation process in Escherichia coli.Microbiology and molecular biology reviews : MMBR · 2007
    Review
  20. 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

5 authors at 3 institutions in 2 countries.

Alexey P KorepanovInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow region, Russia.
George M Gongadze
Maria B Garber
Donald L Court
Mikhail G Bubunenko
Institute of Protein Research · RUFrederick National Laboratory for Cancer Research · USNational Cancer Institute · US

Funding

Recombineering: Chromosome Engineering by Homologous RecZ01BC010336 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI COURT, DONALD · 2000 to 2008
$2.8M
Intramural NIH HHS NIH0010296364Intramural NIH HHS Z01 BC010336Intramural NIH HHS Z99 CA999999NCI NIH HHS N01 CO012400NCI NIH HHS N01-CO-12400
6 · The paper itself

Abstract

A specific complex of 5 S rRNA and several ribosomal proteins is an integral part of ribosomes in all living organisms. Here we studied the importance of Escherichia coli genes rplE, rplR and rplY, encoding 5 S rRNA-binding ribosomal proteins L5, L18 and L25, respectively, for cell growth, viability and translation. Using recombineering to create gene replacements in the E. coli chromosome, it was shown that rplE and rplR are essential for cell viability, whereas cells deleted for rplY are viable, but grow noticeably slower than the parental strain. The slow growth of these L25-defective cells can be stimulated by a plasmid expressing the rplY gene and also by a plasmid bearing the gene for homologous to L25 general stress protein CTC from Bacillus subtilis. The rplY mutant ribosomes are physically normal and contain all ribosomal proteins except L25. The ribosomes from L25-defective and parental cells translate in vitro at the same rate either poly(U) or natural mRNA. The difference observed was that the mutant ribosomes synthesized less natural polypeptide, compared to wild-type ribosomes both in vivo and in vitro. We speculate that the defect is at the ribosome recycling step.

Indexed as

Protein BiosynthesisCell SurvivalCloning, MolecularEscherichia coliEscherichia coli ProteinsMutationRepressor ProteinsRibosomal ProteinsRibosomesRNA, BacterialRNA, Ribosomal, 5STranscription FactorsalsR protein, E coliEscherichia coli ProteinsRepressor Proteinsribosomal protein L5Ribosomal ProteinsRNA, BacterialRNA, Ribosomal, 5STranscription Factors

Identifiers

PMID17198710
PMCPMC1939977
OpenAlexW2014752988

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.