Evidence map›Paper›PMID 21084293›Full record

ArticleThe Journal of biological chemistry2011

Recognition of transcription termination signal by the nuclear polyadenylated RNA-binding (NAB) 3 protein.

Fruzsina Hobor, Roberto Pergoli, Karel Kubicek, Dominika Hrossova, Veronika Bacikova, Michal Zimmermann, Josef Pasulka, Ctirad Hofr, Stepanka Vanacova, Richard Stefl

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

28 citing papers in PubMed, 46 citations in OpenAlex.

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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

10 authors at 2 institutions in 2 countries.

Fruzsina HoborNational Centre for Biomolecular Research, Central European Institute of Technology, Faculty of Science, Masaryk University, Brno CZ-62500, Czechia.
Roberto Pergoli
Karel Kubicek
Dominika Hrossova
Veronika Bacikova
Michal Zimmermann
Josef Pasulka
Ctirad Hofr
Stepanka Vanacova
Richard Stefl
National Centre for Social research · GRCentral European Institute of Technology · CZ

Funding

Howard Hughes Medical InstituteWellcome Trust 084316Wellcome Trust 084316/Z/07/Z
6 · The paper itself

Abstract

Non-coding RNA polymerase II transcripts are processed by the poly(A)-independent termination pathway that requires the Nrd1 complex. The Nrd1 complex includes two RNA-binding proteins, the nuclear polyadenylated RNA-binding (Nab) 3 and the nuclear pre-mRNA down-regulation (Nrd) 1 that bind their specific termination elements. Here we report the solution structure of the RNA-recognition motif (RRM) of Nab3 in complex with a UCUU oligonucleotide, representing the Nab3 termination element. The structure shows that the first three nucleotides of UCUU are accommodated on the β-sheet surface of Nab3 RRM, but reveals a sequence-specific recognition only for the central cytidine and uridine. The specific contacts we identified are important for binding affinity in vitro as well as for yeast viability. Furthermore, we show that both RNA-binding motifs of Nab3 and Nrd1 alone bind their termination elements with a weak affinity. Interestingly, when Nab3 and Nrd1 form a heterodimer, the affinity to RNA is significantly increased due to the cooperative binding. These findings are in accordance with the model of their function in the poly(A) independent termination, in which binding to the combined and/or repetitive termination elements elicits efficient termination.

Indexed as

Transcription, GeneticBase SequenceBinding SitesMagnetic Resonance SpectroscopyNuclear ProteinsOligonucleotidesProtein BindingProtein ConformationProtein MultimerizationRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSolutionsNAB3 protein, S cerevisiaeNRD1 protein, S cerevisiaeNuclear ProteinsOligonucleotidesRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsSolutions

Identifiers

PMID21084293
PMCPMC3030368
OpenAlexW2043862725

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.