Evidence map›Paper›PMID 23636942›Full record

ArticleGenome research2013

Quantitative proteomic analysis reveals concurrent RNA-protein interactions and identifies new RNA-binding proteins in Saccharomyces cerevisiae.

Daniel M Klass, Marion Scheibe, Falk Butter, Gregory J Hogan, Matthias Mann, Patrick O Brown

Open access · bronzeAbstract read
In one paragraph

Article in Genome research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Genome-Wide Analysis ofInternational journal of molecular sciences · 2023
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. A brave new world of RNA-binding proteins.Nature reviews. Molecular cell biology · 2018
    Review
  14. Mbf1 ensures Polycomb silencing by protectingDevelopment (Cambridge, England) · 2018
    Article
  15. Article
  16. Article
  17. RNA Binding by Histone Methyltransferases Set1 and Set2.Molecular and cellular biology · 2017
    Article
  18. Article
  19. Review
  20. Review
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

6 authors at 2 institutions in 2 countries.

Daniel M KlassDepartment of Biochemistry, Stanford University School of Medicine, Stanford, California 94305, USA.
Marion Scheibe
Falk Butter
Gregory J Hogan
Matthias Mann
Patrick O Brown
Howard Hughes Medical Institute · USMax Planck Institute of Biochemistry · DE

Funding

GENE EXPRESSION IN CANCER BY MICROARRAY HYBRIDIZATIONR01CA077097 · NCI · STANFORD UNIVERSITY · PI BROWN, PATRICK O. · 1997 to 2010
$8.7M
Howard Hughes Medical InstituteNCI NIH HHS R01 CA077097NCI NIH HHS R01 CA77097
6 · The paper itself

Abstract

A growing body of evidence supports the existence of an extensive network of RNA-binding proteins (RBPs) whose combinatorial binding affects the post-transcriptional fate of every mRNA in the cell-yet we still do not have a complete understanding of which proteins bind to mRNA, which of these bind concurrently, and when and where in the cell they bind. We describe here a method to identify the proteins that bind to RNA concurrently with an RBP of interest, using quantitative mass spectrometry combined with RNase treatment of affinity-purified RNA-protein complexes. We applied this method to the known RBPs Pab1, Nab2, and Puf3. Our method significantly enriched for known RBPs and is a clear improvement upon previous approaches in yeast. Our data reveal that some reported protein-protein interactions may instead reflect simultaneous binding to shared RNA targets. We also discovered more than 100 candidate RBPs, and we independently confirmed that 77% (23/30) bind directly to RNA. The previously recognized functions of the confirmed novel RBPs were remarkably diverse, and we mapped the RNA-binding region of one of these proteins, the transcriptional coactivator Mbf1, to a region distinct from its DNA-binding domain. Our results also provided new insights into the roles of Nab2 and Puf3 in post-transcriptional regulation by identifying other RBPs that bind simultaneously to the same mRNAs. While existing methods can identify sets of RBPs that interact with common RNA targets, our approach can determine which of those interactions are concurrent-a crucial distinction for understanding post-transcriptional regulation.

Indexed as

Cluster AnalysisModels, BiologicalNucleocytoplasmic Transport ProteinsProtein BindingProteomicsReproducibility of ResultsRNA-Binding ProteinsRNA, MessengerRNA Processing, Post-TranscriptionalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTrans-ActivatorsNAB2 protein, S cerevisiaeNucleocytoplasmic Transport ProteinsPUF3 protein, S cerevisiaeRNA-Binding ProteinsRNA, MessengerSaccharomyces cerevisiae ProteinsTrans-Activators

Identifiers

PMID23636942
PMCPMC3668357
OpenAlexW2025061468

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.