Evidence map›Paper›PMID 25605335›Full record

ArticleMolecular and cellular biology2015

Rbs1, a new protein implicated in RNA polymerase III biogenesis in yeast Saccharomyces cerevisiae.

Małgorzata Cieśla, Ewa Makała, Marta Płonka, Rafał Bazan, Kamil Gewartowski, Andrzej Dziembowski, Magdalena Boguta

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Validation of the Pathogenic Effect ofInternational journal of molecular sciences · 2022
    Article
  6. Review
  7. Article
  8. Biogenesis of RNA Polymerases in Yeast.Frontiers in molecular biosciences · 2021
    Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Maf1 phenotypes and cell physiology.Biochimica et biophysica acta. Gene regulatory mechanisms · 2018
    Review
  17. Review
  18. Article
  19. 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

7 authors at 1 institution in 1 country.

Małgorzata CieślaInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Ewa MakałaInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Marta PłonkaInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Rafał BazanInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Kamil GewartowskiInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland Institute of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, Warsaw, Poland.
Andrzej DziembowskiInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland Institute of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, Warsaw, Poland.
Magdalena BogutaInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland magda@ibb.waw.pl.
Institute of Biochemistry and Biophysics, Polish Academy of Sciences · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Little is known about the RNA polymerase III (Pol III) complex assembly and its transport to the nucleus. We demonstrate that a missense cold-sensitive mutation, rpc128-1007, in the sequence encoding the C-terminal part of the second largest Pol III subunit, C128, affects the assembly and stability of the enzyme. The cellular levels and nuclear concentration of selected Pol III subunits were decreased in rpc128-1007 cells, and the association between Pol III subunits as evaluated by coimmunoprecipitation was also reduced. To identify the proteins involved in Pol III assembly, we performed a genetic screen for suppressors of the rpc128-1007 mutation and selected the Rbs1 gene, whose overexpression enhanced de novo tRNA transcription in rpc128-1007 cells, which correlated with increased stability, nuclear concentration, and interaction of Pol III subunits. The rpc128-1007 rbs1Δ double mutant shows a synthetic growth defect, indicating that rpc128-1007 and rbs1Δ function in parallel ways to negatively regulate Pol III assembly. Rbs1 physically interacts with a subset of Pol III subunits, AC19, AC40, and ABC27/Rpb5. Additionally, Rbs1 interacts with the Crm1 exportin and shuttles between the cytoplasm and nucleus. We postulate that Rbs1 binds to the Pol III complex or subcomplex and facilitates its translocation to the nucleus.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionBase SequenceModels, MolecularMolecular Sequence DataMutationProtein Interaction MapsProtein SubunitsProtein TransportRNA Polymerase IIISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUp-RegulationProtein SubunitsRbs1 protein, S cerevisiaeRNA Polymerase IIISaccharomyces cerevisiae Proteins

Identifiers

PMID25605335
PMCPMC4355530
OpenAlexW2136181016

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.