Evidence map›Paper›PMID 24196969›Full record

ArticleThe Journal of biological chemistry2013

Aminoacylation of Plasmodium falciparum tRNA(Asn) and insights in the synthesis of asparagine repeats.

Denis Filisetti, Anne Théobald-Dietrich, Nassira Mahmoudi, Joëlle Rudinger-Thirion, Ermanno Candolfi, Magali Frugier

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

18 citing papers in PubMed, 35 citations in OpenAlex.

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  15. Apicomplexa-specific tRip facilitates import of exogenous tRNAs into malaria parasites.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
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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

6 authors at 2 institutions in 1 country.

Denis FilisettiFrom the Architecture et Réactivité de l'ARN, Université de Strasbourg, CNRS, Institut de Biologie Moléculaire et Cellulaire, 15 rue René Descartes, 67084 Strasbourg cedex, France and.
Anne Théobald-Dietrich
Nassira Mahmoudi
Joëlle Rudinger-Thirion
Ermanno Candolfi
Magali Frugier
Institut de Biologie Moléculaire et Cellulaire · FRArchitecture et Réactivité de l'arN · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Genome sequencing revealed an extreme AT-rich genome and a profusion of asparagine repeats associated with low complexity regions (LCRs) in proteins of the malarial parasite Plasmodium falciparum. Despite their abundance, the function of these LCRs remains unclear. Because they occur in almost all families of plasmodial proteins, the occurrence of LCRs cannot be associated with any specific metabolic pathway; yet their accumulation must have given selective advantages to the parasite. Translation of these asparagine-rich LCRs demands extraordinarily high amounts of asparaginylated tRNA(Asn). However, unlike other organisms, Plasmodium codon bias is not correlated to tRNA gene copy number. Here, we studied tRNA(Asn) accumulation as well as the catalytic capacities of the asparaginyl-tRNA synthetase of the parasite in vitro. We observed that asparaginylation in this parasite can be considered standard, which is expected to limit the availability of asparaginylated tRNA(Asn) in the cell and, in turn, slow down the ribosomal translation rate when decoding asparagine repeats. This observation strengthens our earlier hypothesis considering that asparagine rich sequences act as "tRNA sponges" and help cotranslational folding of parasite proteins. However, it also raises many questions about the mechanistic aspects of the synthesis of asparagine repeats and about their implications in the global control of protein expression throughout Plasmodium life cycle.

Indexed as

Transfer RNA AminoacylationAmino Acid SequenceAmino Acyl-tRNA SynthetasesAsparagineBacterial ProteinsHumansKineticsMolecular Sequence DataPlasmodium falciparumProtozoan ProteinsPyrococcus abyssiRepetitive Sequences, Amino AcidRNA, Transfer, AsnAmino Acyl-tRNA SynthetasesAsparagineBacterial ProteinsProtozoan ProteinsRNA, Transfer, AsnAminoacyl tRNA SynthesisAsparagine RepeatsLow Complexity RegionsPlasmodiumProtein FoldingTransfer RNA (tRNA)Translation

Identifiers

PMID24196969
PMCPMC3868750
OpenAlexW2049797818

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.