Evidence map›Paper›PMID 25364902›Full record

ArticlePloS one2014

Genome-wide analyses and functional classification of proline repeat-rich proteins: potential role of eIF5A in eukaryotic evolution.

Ajeet Mandal, Swati Mandal, Myung Hee Park

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

53 citing papers in PubMed, 97 citations in OpenAlex.

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  17. Spermidine and spermine exert protective effects within the lung.Pharmacology research & perspectives · 2021
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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

3 authors at 2 institutions in 1 country.

Ajeet MandalOral and Pharyngeal Cancer Branch, NIDCR, National Institutes of Health, Bethesda, Maryland, United States of America.
Swati MandalOral and Pharyngeal Cancer Branch, NIDCR, National Institutes of Health, Bethesda, Maryland, United States of America.
Myung Hee ParkOral and Pharyngeal Cancer Branch, NIDCR, National Institutes of Health, Bethesda, Maryland, United States of America.
National Institute of Dental and Craniofacial Research · USNational Institutes of Health · US

Funding

The Post-translational Synthesis of Hypusine In eIF5A and roles of eIF5A and polyamines in cell growth and animal developmentZIADE000608 · NIDCR · NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH · PI PARK, MYUNG HEE · 2009 to 2021
$12.3M
Intramural NIH HHS
6 · The paper itself

Abstract

The eukaryotic translation factor, eIF5A has been recently reported as a sequence-specific elongation factor that facilitates peptide bond formation at consecutive prolines in Saccharomyces cerevisiae, as its ortholog elongation factor P (EF-P) does in bacteria. We have searched the genome databases of 35 representative organisms from six kingdoms of life for PPP (Pro-Pro-Pro) and/or PPG (Pro-Pro-Gly)-encoding genes whose expression is expected to depend on eIF5A. We have made detailed analyses of proteome data of 5 selected species, Escherichia coli, Saccharomyces cerevisiae, Drosophila melanogaster, Mus musculus and Homo sapiens. The PPP and PPG motifs are low in the prokaryotic proteomes. However, their frequencies markedly increase with the biological complexity of eukaryotic organisms, and are higher in newly derived proteins than in those orthologous proteins commonly shared in all species. Ontology classifications of S. cerevisiae and human genes encoding the highest level of polyprolines reveal their strong association with several specific biological processes, including actin/cytoskeletal associated functions, RNA splicing/turnover, DNA binding/transcription and cell signaling. Previously reported phenotypic defects in actin polarity and mRNA decay of eIF5A mutant strains are consistent with the proposed role for eIF5A in the translation of the polyproline-containing proteins. Of all the amino acid tandem repeats (≥3 amino acids), only the proline repeat frequency correlates with functional complexity of the five organisms examined. Taken together, these findings suggest the importance of proline repeat-rich proteins and a potential role for eIF5A and its hypusine modification pathway in the course of eukaryotic evolution.

Indexed as

Evolution, MolecularGenome-Wide Association StudyPeptidesProline-Rich Protein DomainsAnimalsDatabases, ProteinDrosophila melanogasterDrosophila ProteinsEscherichia coliEscherichia coli ProteinsEukaryotic Translation Initiation Factor 5AHumansMicePeptide Initiation FactorsRepetitive Sequences, Amino AcidRNA-Binding ProteinsDrosophila ProteinsEscherichia coli ProteinsEukaryotic Translation Initiation Factor 5APeptide Initiation FactorsPeptidespolyprolineRNA-Binding ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID25364902
PMCPMC4218817
OpenAlexW2094154815

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Registered trials

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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.