Evidence map›Paper›PMID 24214533›Full record

ArticlePlant physiology2014

RBF1, a plant homolog of the bacterial ribosome-binding factor RbfA, acts in processing of the chloroplast 16S ribosomal RNA.

Rikard Fristedt, Lars B Scharff, Cornelia A Clarke, Qin Wang, Chentao Lin, Sabeeha S Merchant, Ralph Bock

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

30 citing papers in PubMed, 52 citations in OpenAlex.

  1. The Elements of Life, Photosynthesis and Genomics.Journal of molecular biology · 2025
    Review
  2. Article
  3. Article
  4. Plant organellar RNA maturation.The Plant cell · 2023
    Review
  5. Article
  6. Review
  7. Article
  8. Mutation of theFrontiers in plant science · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
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  17. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Rikard FristedtDepartment of Chemistry and Biochemistry , University of California, Los Angeles, California 90095.
Lars B Scharff
Cornelia A Clarke
Qin Wang
Chentao Lin
Sabeeha S Merchant
Ralph Bock
United States Nuclear Regulatory Commission · USMax Planck Institute of Molecular Plant Physiology · DE

Funding

The signaling mechanisms of Arabidopsis CRY2R01GM056265 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LIN, CHENTAO · 2001 to 2021
$9.5M
NIGMS NIH HHS R01 GM056265
6 · The paper itself

Abstract

Plastids (chloroplasts) possess 70S ribosomes that are very similar in structure and function to the ribosomes of their bacterial ancestors. While most components of the bacterial ribosome (ribosomal RNAs [rRNAs] and ribosomal proteins) are well conserved in the plastid ribosome, little is known about the factors mediating the biogenesis of plastid ribosomes. Here, we have investigated a putative homolog of the bacterial RbfA (for ribosome-binding factor A) protein that was identified as a cold-shock protein and an auxiliary factor acting in the 5' maturation of the 16S rRNA. The unicellular green alga Chlamydomonas reinhardtii and the vascular plant Arabidopsis (Arabidopsis thaliana) both encode a single RbfA-like protein in their nuclear genomes. By generating specific antibodies against this protein, we show that the plant RbfA-like protein functions exclusively in the plastid, where it is associated with thylakoid membranes. Analysis of mutants for the corresponding gene (termed RBF1) reveals that the gene function is essential for photoautotrophic growth. Weak mutant alleles display reduced levels of plastid ribosomes, a specific depletion in 30S ribosomal subunits, and reduced activity of plastid protein biosynthesis. Our data suggest that, while the function in ribosome maturation and 16S rRNA 5' end processing is conserved, the RBF1 protein has assumed an additional role in 3' end processing. Together with the apparent absence of a homologous protein from plant mitochondria, our findings illustrate that the assembly process of the 70S ribosome is not strictly conserved and has undergone some modifications during organelle evolution.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsChlamydomonas reinhardtiiChloroplastsEscherichia coli ProteinsGenetic Complementation TestMolecular Sequence DataMutationPhotosynthesisPlants, Genetically ModifiedPlastidsRibosomal ProteinsRNA, Ribosomal, 16SSequence Homology, Amino AcidThylakoidsArabidopsis ProteinsEscherichia coli ProteinsRbfA protein, E coliRibosomal ProteinsRNA, Ribosomal, 16S

Identifiers

PMID24214533
PMCPMC3875801
OpenAlexW2051612911

What OpenQuestion holds

Textmetadata
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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.