Evidence map›Paper›PMID 31104813›Full record

ArticleStructure (London, England : 1993)2019

Identification of Three Sequence Motifs in the Transcription Termination Factor Sen1 that Mediate Direct Interactions with Nrd1.

Yinglu Zhang, Yujin Chun, Stephen Buratowski, Liang Tong

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Structure (London, England : 1993), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
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  4. Review
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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

4 authors at 2 institutions in 1 country.

Yinglu ZhangDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA.
Yujin ChunDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Stephen BuratowskiDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Liang TongDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA. Electronic address: ltong@columbia.edu.
Columbia University · USHarvard University · US

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
The RNA Polymerase II Transcription CycleR01GM056663 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI Stephen Buratowski · 1999 to 2026
$11.7M
Structural and functional studies of mRNA processing, stability and quality controlR35GM118093 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI LIANG TONG · 2016 to 2026
$8.5M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
Replacement of an aging X-ray diffraction system for protein crystallographyS10OD012018 · OD · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI TONG, LIANG · 2012 to 2012
$405k
NCRR NIH HHS S10 RR029205NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM056663NIGMS NIH HHS R35 GM118093NIH HHS S10 OD012018
6 · The paper itself

Abstract

The Nrd1-Nab3-Sen1 (NNS) complex carries out the transcription termination of non-coding RNAs (ncRNAs) by RNA polymerase II (Pol II) in yeast, although the detailed interactions among its subunits remain obscure. Here we have identified three sequence motifs in Sen1 that mediate direct interactions with the Pol II CTD interaction domain (CID) of Nrd1, determined the crystal structures of these Nrd1 interaction motifs (NIMs) bound to the CID, and characterized the interactions in vitro and in yeast. Removal of all three NIMs abolishes NNS complex formation and gives rise to ncRNA termination defects.

Indexed as

Transcription Termination, GeneticAmino Acid MotifsBinding SitesCloning, MolecularCrystallography, X-RayDNA HelicasesEscherichia coliGene ExpressionGenetic VectorsModels, MolecularNuclear ProteinsProtein BindingProtein Conformation, alpha-HelicalProtein Interaction Domains and MotifsProtein MultimerizationRecombinant ProteinsDNA HelicasesNAB3 protein, S cerevisiaeNRD1 protein, S cerevisiaeNuclear ProteinsRecombinant ProteinsRNA-Binding ProteinsRNA HelicasesRNA Polymerase IIRNA, UntranslatedSaccharomyces cerevisiae ProteinsSEN1 protein, S cerevisiaenon-coding RNAprotein complexprotein structuretranscription termination

Identifiers

PMID31104813
PMCPMC6610696
OpenAlexW2904725023

What OpenQuestion holds

Textmetadata
LicenceTDM
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.