Evidence map›Paper›PMID 11121078›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Completing the heterotrimer: isolation and characterization of an Arabidopsis thaliana G protein gamma-subunit cDNA.

M G Mason, J R Botella

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
–field-weighted citation impact
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

82 citing papers in PubMed.

  1. Article
  2. Article
  3. Genome-Wide Identification of thePlants (Basel, Switzerland) · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. G-Protein β-Subunit GeneInternational journal of molecular sciences · 2023
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Heterotrimeric G Proteins in Plants: Canonical and Atypical Gα Subunits.International journal of molecular sciences · 2021
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Characterization of Heterotrimeric G Protein γ4 Subunit in Rice.International journal of molecular sciences · 2018
    Article
  19. Article
  20. Article

22 more citing papers are in PubMed but not listed here.

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

2 authors.

M G MasonPlant Genetic Engineering Laboratory, Department of Botany, University of Queensland, Brisbane, Queensland 4072, Australia.
J R Botella

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heterotrimeric G proteins consist of three subunits (alpha, beta, and gamma). alpha- and beta- subunits have been previously cloned in plants, but the gamma-subunit has remained elusive. To isolate the gamma-subunit of a plant heterotrimeric G protein an Arabidopsis thaliana yeast two-hybrid library was screened by using a tobacco G-beta-subunit as the bait protein. One positive clone (AGG1) was isolated several times; it displays significant homology to the conserved domains of mammalian gamma-subunits. The predicted AGG1 protein sequence contains all of the typical characteristics of mammalian gamma-subunits such as small size (98 amino acids, 10.8 kDa), presence of a C-terminal CAAX box to direct isoprenyl modification, and an N-terminal alpha-helix region capable of forming a coiled-coil interaction with the beta-subunit. Northern and Southern analyses showed that AGG1 is a single-copy gene in Arabidopsis with a similar expression pattern to the Arabidopsis beta-subunit, AGB1 [Weiss, C. A., Garnaat, C. W., Mukai, K., Hu, Y. & Ma, H. (1994) Proc. Natl. Acad. Sci. USA 91, 9554-9558]. By using the yeast two-hybrid system, we show that AGG1 strongly interacts with tobacco and Arabidopsis beta-subunits. The in vivo results have been confirmed by using in vitro methods to prove the interaction between AGG1 and the Arabidopsis beta-subunit. As previously observed in mammalian systems, both the coiled-coil domain and the WD repeat regions of the beta-subunit are essential for AGG1 interaction. Also in agreement with previous observations, the removal of the N-terminal alpha-helix of the AGG1 greatly reduces but does not completely block the interaction.

Indexed as

Genes, PlantAmino Acid SequenceAnimalsArabidopsisArabidopsis ProteinsBase SequenceDNA, ComplementaryDNA, PlantGene DosageGene Expression ProfilingGTP-Binding Protein gamma SubunitsMolecular Sequence DataSequence Analysis, DNASequence Homology, Amino AcidAGG1 protein, ArabidopsisArabidopsis ProteinsDNA, ComplementaryDNA, PlantGTP-Binding Protein gamma Subunits

Identifiers

PMID11121078
PMCPMC18996

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.