Evidence map›Paper›PMID 25793367›Full record

ArticlePloS one2015

Multiple RNA processing defects and impaired chloroplast function in plants deficient in the organellar protein-only RNase P enzyme.

Wenbin Zhou, Daniel Karcher, Axel Fischer, Eugenia Maximova, Dirk Walther, Ralph Bock

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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Plant organellar RNA maturation.The Plant cell · 2023
    Review
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  11. TheRNA (New York, N.Y.) · 2018
    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.

Wenbin ZhouMax-Planck-Institut für Molekulare Pflanzenphysiologie, Potsdam-Golm, Germany.
Daniel KarcherMax-Planck-Institut für Molekulare Pflanzenphysiologie, Potsdam-Golm, Germany.
Axel FischerMax-Planck-Institut für Molekulare Pflanzenphysiologie, Potsdam-Golm, Germany.
Eugenia MaximovaMax-Planck-Institut für Molekulare Pflanzenphysiologie, Potsdam-Golm, Germany.
Dirk WaltherMax-Planck-Institut für Molekulare Pflanzenphysiologie, Potsdam-Golm, Germany.
Ralph BockMax-Planck-Institut für Molekulare Pflanzenphysiologie, Potsdam-Golm, Germany.
Max Planck Institute of Molecular Plant Physiology · DEMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transfer RNA (tRNA) precursors undergo endoribonucleolytic processing of their 5' and 3' ends. 5' cleavage of the precursor transcript is performed by ribonuclease P (RNase P). While in most organisms RNase P is a ribonucleoprotein that harbors a catalytically active RNA component, human mitochondria and the chloroplasts (plastids) and mitochondria of seed plants possess protein-only RNase P enzymes (PRORPs). The plant organellar PRORP (PRORP1) has been characterized to some extent in vitro and by transient gene silencing, but the molecular, phenotypic and physiological consequences of its down-regulation in stable transgenic plants have not been assessed. Here we have addressed the function of the dually targeted organellar PRORP enzyme in vivo by generating stably transformed Arabidopsis plants in which expression of the PRORP1 gene was suppressed by RNA interference (RNAi). PRORP1 knock-down lines show defects in photosynthesis, while mitochondrial respiration is not appreciably affected. In both plastids and mitochondria, the effects of PRORP1 knock-down on the processing of individual tRNA species are highly variable. The drastic reduction in the levels of mature plastid tRNA-Phe(GAA) and tRNA-Arg(ACG) suggests that these two tRNA species limit plastid gene expression in the PRORP1 mutants and, hence, are causally responsible for the mutant phenotype.

Indexed as

RNA Processing, Post-TranscriptionalArabidopsisArabidopsis ProteinsChloroplastsMitochondriaMutationPhotosynthesisRibonuclease PRNA, MessengerArabidopsis ProteinsPRORP1 protein, ArabidopsisRibonuclease PRNA, Messenger

Identifiers

PMID25793367
PMCPMC4368725
OpenAlexW2045352663

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.