Evidence map›Paper›PMID 22821559›Full record

ArticleNucleic acids research2012

Protein L5 is crucial for in vivo assembly of the bacterial 50S ribosomal subunit central protuberance.

Alexey P Korepanov, Anna V Korobeinikova, Sergey A Shestakov, Maria B Garber, George M Gongadze

Abstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
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

12 citing papers in PubMed.

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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.

Alexey P KorepanovInstitute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region 142290, Russia. korepan@vega.protres.ru
Anna V Korobeinikova
Sergey A Shestakov
Maria B Garber
George M Gongadze

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the present work, ribosomes assembled in bacterial cells in the absence of essential ribosomal protein L5 were obtained. After arresting L5 synthesis, Escherichia coli cells divide a limited number of times. During this time, accumulation of defective large ribosomal subunits occurs. These 45S particles lack most of the central protuberance (CP) components (5S rRNA and proteins L5, L16, L18, L25, L27, L31, L33 and L35) and are not able to associate with the small ribosomal subunit. At the same time, 5S rRNA is found in the cytoplasm in complex with ribosomal proteins L18 and L25 at quantities equal to the amount of ribosomes. Thus, it is the first demonstration that protein L5 plays a key role in formation of the CP during assembly of the large ribosomal subunit in the bacterial cell. A possible model for the CP assembly in vivo is discussed in view of the data obtained.

Indexed as

Escherichia coliEscherichia coli ProteinsGene DeletionModels, MolecularRibosomal ProteinsRibosomesRibosome Subunits, Large, BacterialRNA, Ribosomal, 5SEscherichia coli Proteinsribosomal protein L5Ribosomal ProteinsRNA, Ribosomal, 5SRplE protein, E coli

Identifiers

PMID22821559
PMCPMC3467071

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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.