Evidence map›Paper›PMID 25625317›Full record

ArticlePloS one2015

Mutations in ribosomal proteins, RPL4 and RACK1, suppress the phenotype of a thermospermine-deficient mutant of Arabidopsis thaliana.

Jun-ichi Kakehi, Eri Kawano, Kaori Yoshimoto, Qingqing Cai, Akihiro Imai, Taku Takahashi

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed, 1 pooled it
7.2field-weighted citation impact, top 4% 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

23 citing papers in PubMed, 1 synthesis or guideline pooled it, 38 citations in OpenAlex.

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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 1 institution in 1 country.

Jun-ichi KakehiGraduate School of Natural Science and Technology, Okayama University, Okayama, Japan.
Eri KawanoGraduate School of Natural Science and Technology, Okayama University, Okayama, Japan.
Kaori YoshimotoGraduate School of Natural Science and Technology, Okayama University, Okayama, Japan.
Qingqing CaiGraduate School of Natural Science and Technology, Okayama University, Okayama, Japan.
Akihiro ImaiGraduate School of Natural Science and Technology, Okayama University, Okayama, Japan.
Taku TakahashiGraduate School of Natural Science and Technology, Okayama University, Okayama, Japan.
Okayama University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thermospermine acts in negative regulation of xylem differentiation and its deficient mutant of Arabidopsis thaliana, acaulis5 (acl5), shows excessive xylem formation and severe dwarfism. Studies of two dominant suppressors of acl5, sac51-d and sac52-d, have revealed that SAC51 and SAC52 encode a transcription factor and a ribosomal protein L10 (RPL10), respectively, and these mutations enhance translation of the SAC51 mRNA, which contains conserved upstream open reading frames in the 5' leader. Here we report identification of SAC53 and SAC56 responsible for additional suppressors of acl5. sac53-d is a semi-dominant allele of the gene encoding a receptor for activated C kinase 1 (RACK1) homolog, a component of the 40S ribosomal subunit. sac56-d represents a semi-dominant allele of the gene for RPL4. We show that the GUS reporter activity driven by the CaMV 35S promoter plus the SAC51 5' leader is reduced in acl5 and restored by sac52-d, sac53-d, and sac56-d as well as thermospermine. Furthermore, the SAC51 mRNA, which may be a target of nonsense-mediated mRNA decay, was found to be stabilized in these ribosomal mutants and by thermospermine. These ribosomal proteins are suggested to act in the control of uORF-mediated translation repression of SAC51, which is derepressed by thermospermine.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsBasic Helix-Loop-Helix ProteinsGene ExpressionGenes, DominantMolecular Sequence DataMutationPhenotypeReceptors, Cell SurfaceReceptors for Activated C KinaseRibosomal Protein L10Ribosomal ProteinsRNA StabilityArabidopsis ProteinsBasic Helix-Loop-Helix ProteinsRACK1 protein, ArabidopsisReceptors, Cell SurfaceReceptors for Activated C Kinaseribosomal protein L10, Arabidopsisribosomal protein L4Ribosomal ProteinsSAC51 protein, Arabidopsis

Identifiers

PMID25625317
PMCPMC4308196
OpenAlexW2031277936

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.