Evidence map›Paper›PMID 19448108›Full record

ArticleEukaryotic cell2009

Saccharomyces cerevisiae Rbg1 protein and its binding partner Gir2 interact on Polyribosomes with Gcn1.

P K Wout, E Sattlegger, S M Sullivan, J R Maddock

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

21 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Article
  3. Emerging Role of GCN1 in Disease and Homeostasis.International journal of molecular sciences · 2024
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Developmentally regulated GTPases: structure, function and roles in disease.Cellular and molecular life sciences : CMLS · 2021
    Review
  11. Article
  12. Structure of Gcn1 bound to stalled and colliding 80S ribosomes.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Ribo-Seq and RNA-Seq ofF1000Research · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. The universally conserved prokaryotic GTPases.Microbiology and molecular biology reviews : MMBR · 2011
    Review
  20. 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

4 authors at 2 institutions in 2 countries.

P K WoutDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109-1048, USA.
E Sattlegger
S M Sullivan
J R Maddock
University of Michigan–Ann Arbor · USMassey University · NZ

Funding

In vivo Assembly of the Large Ribosomal SubunitR01GM077628 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MADDOCK, JANINE R. · 2008 to 2011
$1.0M
NIGMS NIH HHS GM077628NIGMS NIH HHS R01 GM077628
6 · The paper itself

Abstract

Rbg1 is a previously uncharacterized protein of Saccharomyces cerevisiae belonging to the Obg/CgtA subfamily of GTP-binding proteins whose members are involved in ribosome function in both prokaryotes and eukaryotes. We show here that Rbg1 specifically associates with translating ribosomes. In addition, in this study proteins were identified that interact with Rbg1 by yeast two-hybrid screening and include Tma46, Ygr250c, Yap1, and Gir2. Gir2 contains a GI (Gcn2 and Impact) domain similar to that of Gcn2, an essential factor of the general amino acid control pathway required for overcoming amino acid shortage. Interestingly, we found that Gir2, like Gcn2, interacts with Gcn1 through its GI domain, and overexpression of Gir2, under conditions mimicking amino acid starvation, resulted in inhibition of growth that could be reversed by Gcn2 co-overexpression. Moreover, we found that Gir2 also cofractionated with polyribosomes, and this fractionation pattern was partially dependent on the presence of Gcn1. Based on these findings, we conclude that Rbg1 and its interacting partner Gir2 associate with ribosomes, and their possible biological roles are discussed.

Indexed as

Amino AcidsBinding SitesCarrier ProteinsGene Expression Regulation, FungalGTP-Binding ProteinsPeptide Elongation FactorsProtein BindingProtein BiosynthesisProtein Structure, TertiaryRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionAmino AcidsCarrier ProteinsGCN1 protein, S cerevisiaeGir2 protein, S cerevisiaeGTP-Binding ProteinsPeptide Elongation FactorsRbg1 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID19448108
PMCPMC2708457
OpenAlexW2116145278

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.