Evidence map›Paper›PMID 16581807›Full record

ArticleRNA (New York, N.Y.)2006

The La protein functions redundantly with tRNA modification enzymes to ensure tRNA structural stability.

Laura A Copela, Ghadiyaram Chakshusmathi, R Lynn Sherrer, Sandra L Wolin

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

46 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
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  5. RNA modifying enzymes shape tRNA biogenesis and function.The Journal of biological chemistry · 2024
    Review
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  8. Human TRMT1 catalyzes mScience China. Life sciences · 2023
    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

4 authors at 1 institution in 1 country.

Laura A CopelaDepartment of Cell Biology, Howard Hughes Medical Institute, Yale University School of Medicine, 295 Congress Avenue, New Haven, Connecticut 06536, USA.
Ghadiyaram Chakshusmathi
R Lynn Sherrer
Sandra L Wolin
Howard Hughes Medical Institute · US

Funding

Biogenesis of Small RNAsR01GM048410 · NIGMS · YALE UNIVERSITY · PI WOLIN, SANDRA L. · 1998 to 2009
$2.2M
NIGMS NIH HHS R01 GM048410NIGMS NIH HHS R01-GM48410
6 · The paper itself

Abstract

Although the La protein stabilizes nascent pre-tRNAs from nucleases, influences the pathway of pre-tRNA maturation, and assists correct folding of certain pre-tRNAs, it is dispensable for growth in both budding and fission yeast. Here we show that the Saccharomyces cerevisiae La shares functional redundancy with both tRNA modification enzymes and other proteins that contact tRNAs during their biogenesis. La is important for growth in the presence of mutations in either the arginyl tRNA synthetase or the tRNA modification enzyme Trm1p. In addition, two pseudouridine synthases, PUS3 and PUS4, are important for growth in strains carrying a mutation in tRNA(Arg)(CCG) and are essential when La is deleted in these strains. Depletion of Pus3p results in accumulation of the aminoacylated mutant tRNA(Arg)(CCG) in nuclei, while depletion of Pus4p results in decreased stability of the mutant tRNA. Interestingly, the degradation of mutant unstable forms of tRNA(Arg)(CCG) does not require the Trf4p poly(A) polymerase, suggesting that yeast cells possess multiple pathways for tRNA decay. These data demonstrate that La functions redundantly with both tRNA modifications and proteins that associate with tRNAs to achieve tRNA structural stability and efficient biogenesis.

Indexed as

Nucleic Acid ConformationAmino Acyl-tRNA SynthetasesBase SequenceBlotting, NorthernDNA PrimersIn Situ HybridizationMutagenesisPlasmidsRNA, Transfer, ArgSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinstRNA MethyltransferasesAmino Acyl-tRNA SynthetasesDNA PrimersRNA, Transfer, ArgSaccharomyces cerevisiae ProteinstRNA Methyltransferases

Identifiers

PMID16581807
PMCPMC1421099
OpenAlexW2119774438

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.