Evidence map›Paper›PMID 19636801›Full record

ArticlePlant molecular biology2009

AtObgC, a plant ortholog of bacterial Obg, is a chloroplast-targeting GTPase essential for early embryogenesis.

Woo Young Bang, Akira Hata, In Sil Jeong, Tetsuya Umeda, Takayuki Masuda, Ji Chen, Ishizaki Yoko, I Nengah Suwastika, Dae Won Kim, Chak Han Im and 5 more

Abstract read
PubMed Publisher
In one paragraph

Article in Plant molecular biology, 2009. 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
1.6field-weighted citation impact, top 17% 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, 42 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Chloroplast vesicle transport.Photosynthesis research · 2018
    Review
  5. RiceG3 (Bethesda, Md.) · 2018
    Article
  6. Structural and biochemical analysis ofThe Journal of biological chemistry · 2017
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. The universally conserved prokaryotic GTPases.Microbiology and molecular biology reviews : MMBR · 2011
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
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

15 authors at 3 institutions in 2 countries.

Woo Young BangDivision of Applied Life Sciences (BK21 and EB-NCRC), Graduate School of Gyeongsang National University, Jinju 660-701, Korea.
Akira Hata
In Sil Jeong
Tetsuya Umeda
Takayuki Masuda
Ji Chen
Ishizaki Yoko
I Nengah Suwastika
Dae Won Kim
Chak Han Im
Byung Hyun Lee
Yuno Lee
Keun Woo Lee
Takashi Shiina
Jeong Dong Bahk
Gyeongsang National University · KRKyoto Prefectural University · JPKyoto University of Education · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Obg is a ribosome-associated GTPase essential for bacterial viability and is conserved in most organisms, from bacteria to eukaryotes. Obg is also expressed in plants, which predicts an important role for this molecule in plant viability; however, the functions of the plant Obg homologs have not been reported. Here, we first identified Arabidopsis AtObgC as a plant chloroplast-targeting Obg and elucidated its molecular biological and physiological properties. AtObgC encodes a plant-specific Obg GTPase that contains an N-terminal region for chloroplast targeting and has intrinsic GTP hydrolysis activity. A targeting assay using a few AtObgC N-terminal truncation mutants revealed that AtObgC localizes to chloroplasts and its transit peptide consists of more than 50 amino acid residues. Interestingly, GFP-fused full-length AtObgC exhibited a punctate staining pattern in chloroplasts of Arabidopsis protoplasts, which suggests a dimerization or multimerization of AtObgC. Moreover, its Obg fold was indispensable for the generation of the punctate staining pattern, and thus, was supposed to be important for such oligomerization of AtObgC by mediating the protein-protein interaction. In addition, the T-DNA insertion AtObgC null mutant exhibited an embryonic lethal phenotype that disturbed the early stage of embryogenesis. Altogether, our results provide a significant implication that AtObgC as a chloroplast targeting GTPase plays an important role at the early embryogenesis by exerting its function in chloroplast protein synthesis.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsBacterial ProteinsChloroplastsGene Expression Regulation, PlantGTP-Binding ProteinsGTP PhosphohydrolasesMolecular Sequence DataPhylogenyPlants, Genetically ModifiedSequence AlignmentSequence Homology, Amino AcidArabidopsis ProteinsBacterial ProteinsGTP-Binding ProteinsGTP PhosphohydrolasesObg GTP-binding protein, Bacteria

Identifiers

PMID19636801
OpenAlexW2139442663

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.