Evidence map›Paper›PMID 31777937›Full record

ArticleNucleic acids research2020

A novel 5'-hydroxyl dinucleotide hydrolase activity for the DXO/Rai1 family of enzymes.

Selom K Doamekpor, Agnieszka Gozdek, Aleksandra Kwasnik, Joanna Kufel, Liang Tong

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.7field-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

15 citing papers in PubMed, 25 citations in OpenAlex.

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  12. Comparative parallel analysis of RNA ends identifies mRNA substrates of a tRNA splicing endonuclease-initiated mRNA decay pathway.Proceedings of the National Academy of Sciences of the United States of America · 2021
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Selom K DoamekporDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA.
Agnieszka GozdekInstitute of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, 02-106 Warsaw, Poland.
Aleksandra KwasnikInstitute of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, 02-106 Warsaw, Poland.
Joanna KufelInstitute of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, 02-106 Warsaw, Poland.
Liang TongDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA.
University of Warsaw · PLColumbia University · US

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
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
Replacement of an aging X-ray diffraction system for protein crystallographyS10OD012018 · OD · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI TONG, LIANG · 2012 to 2012
$405k
NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R35 GM118093NIH HHS S10 OD012018
6 · The paper itself

Abstract

Modifications at the 5'-end of RNAs play a pivotal role in determining their fate. In eukaryotes, the DXO/Rai1 family of enzymes removes numerous 5'-end RNA modifications, thereby regulating RNA turnover. Mouse DXO catalyzes the elimination of incomplete 5'-end caps (including pyrophosphate) and the non-canonical NAD+ cap on mRNAs, and possesses distributive 5'-3' exoribonuclease activity toward 5'-monophosphate (5'-PO4) RNA. Here, we demonstrate that DXO also catalyzes the hydrolysis of RNAs bearing a 5'-hydroxyl group (5'-OH RNA). The crystal structure of DXO in complex with a 5'-OH RNA substrate mimic at 2.0 Å resolution provides elegant insight into the molecular mechanism of this activity. More importantly, the structure predicts that DXO first removes a dinucleotide from 5'-OH RNA. Our nuclease assays confirm this prediction and demonstrate that this 5'-hydroxyl dinucleotide hydrolase (HDH) activity for DXO is higher than the subsequent 5'-3' exoribonuclease activity for selected substrates. Fission yeast Rai1 also has HDH activity although it does not have 5'-3' exonuclease activity, and the Rat1-Rai1 complex can completely degrade 5'-OH RNA. An Arabidopsis DXO1 variant is active toward 5'-OH RNA but prefers 5'-PO4 RNA. Collectively, these studies demonstrate the diverse activities of DXO/Rai1 and expands the collection of RNA substrates that can undergo 5'-3' mediated decay.

Indexed as

AnimalsArabidopsisArabidopsis ProteinsBinding SitesChloroplast ProteinsCloning, MolecularCrystallography, X-RayEscherichia coliExoribonucleasesGene ExpressionGenetic VectorsMiceModels, MolecularNuclear ProteinsProtein BindingProtein Conformation, alpha-HelicalArabidopsis ProteinsAT4G17620 protein, ArabidopsisChloroplast ProteinsDom3Z protein, mouseExoribonucleasesNuclear ProteinsRai1 protein, mouseRai1 protein, S cerevisiaeRAT1 protein, S cerevisiaeRecombinant ProteinsRNA-Binding ProteinsRNA, MessengerSaccharomyces cerevisiae ProteinsTrans-Activators

Identifiers

PMID31777937
PMCPMC6943137
OpenAlexW2991289753

What OpenQuestion holds

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LicenceCC BY
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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.