Evidence map›Paper›PMID 15024427›Full record

ArticlePLoS biology2004

Extensive association of functionally and cytotopically related mRNAs with Puf family RNA-binding proteins in yeast.

André P Gerber, Daniel Herschlag, Patrick O Brown

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 385 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
385citing papers in PubMed, 1 pooled it
13.5field-weighted citation impact, top 1% 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

385 citing papers in PubMed, 1 synthesis or guideline pooled it, 666 citations in OpenAlex.

  1. Pooled it
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  10. RNA (New York, N.Y.) · 2025
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325 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

3 authors at 2 institutions in 1 country.

André P GerberDepartment of Biochemistry, Stanford University School of Medicine, Stanford, California, USA.
Daniel Herschlag
Patrick O Brown
Stanford University · USHoward Hughes Medical Institute · US

Funding

Enzymology of a Catalytic RNA MoleculeR37GM049243 · NIGMS · STANFORD UNIVERSITY · PI HERSCHLAG, DANIEL · 2002 to 2011
$4.2M
ENZYMOLOGY OF A CATALYTIC RNA MOLECULER01GM049243 · NIGMS · STANFORD UNIVERSITY · PI HERSCHLAG, DANIEL · 1993 to 2016
$2.3M
NIGMS NIH HHS GM49243NIGMS NIH HHS R01 GM049243NIGMS NIH HHS R37 GM049243
6 · The paper itself

Abstract

Genes encoding RNA-binding proteins are diverse and abundant in eukaryotic genomes. Although some have been shown to have roles in post-transcriptional regulation of the expression of specific genes, few of these proteins have been studied systematically. We have used an affinity tag to isolate each of the five members of the Puf family of RNA-binding proteins in Saccharomyces cerevisiae and DNA microarrays to comprehensively identify the associated mRNAs. Distinct groups of 40-220 different mRNAs with striking common themes in the functions and subcellular localization of the proteins they encode are associated with each of the five Puf proteins: Puf3p binds nearly exclusively to cytoplasmic mRNAs that encode mitochondrial proteins; Puf1p and Puf2p interact preferentially with mRNAs encoding membrane-associated proteins; Puf4p preferentially binds mRNAs encoding nucleolar ribosomal RNA-processing factors; and Puf5p is associated with mRNAs encoding chromatin modifiers and components of the spindle pole body. We identified distinct sequence motifs in the 3'-untranslated regions of the mRNAs bound by Puf3p, Puf4p, and Puf5p. Three-hybrid assays confirmed the role of these motifs in specific RNA-protein interactions in vivo. The results suggest that combinatorial tagging of transcripts by specific RNA-binding proteins may be a general mechanism for coordinated control of the localization, translation, and decay of mRNAs and thus an integral part of the global gene expression program.

Indexed as

3' Untranslated RegionsAmino Acid MotifsAnimalsCell Cycle ProteinsChromatinCytoplasmDNA PrimersFungal ProteinsGene Expression ProfilingGene Expression Regulation, FungalGenes, FungalMembrane ProteinsMicroscopy, FluorescenceMitochondriaMolecular Sequence DataNucleic Acid Hybridization3' Untranslated RegionsCell Cycle ProteinsChromatinDNA PrimersFungal ProteinsJSN1 protein, S cerevisiaeMembrane ProteinsMPT5 protein, S cerevisiaePUF2 protein, S cerevisiaePUF3 protein, S cerevisiaePUF4 protein, S cerevisiaeRepressor ProteinsRNARNA-Binding ProteinsRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID15024427
PMCPMC368173
OpenAlexW2049402769

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.