Evidence map›Paper›PMID 30507380›Full record

ArticleeLife2018

Biosynthesis of histone messenger RNA employs a specific 3' end endonuclease.

Ilaria Pettinati, Pawel Grzechnik, Claudia Ribeiro de Almeida, Jurgen Brem, Michael A McDonough, Somdutta Dhir, Nick J Proudfoot, Christopher J Schofield

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

9 citing papers in PubMed, 17 citations in OpenAlex.

  1. GlialProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Article
  3. Article
  4. Enhanced Thermostability of D-Psicose 3-Epimerase fromInternational journal of molecular sciences · 2021
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
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

8 authors at 2 institutions in 1 country.

Ilaria PettinatiDepartment of Chemistry, University of Oxford, Oxford, United Kingdom.ORCID 0000-0002-5904-7984
Pawel GrzechnikSchool of Biosciences, University of Birmingham, Birmingham, United Kingdom.ORCID 0000-0003-3355-1741
Claudia Ribeiro de AlmeidaSir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.
Jurgen BremDepartment of Chemistry, University of Oxford, Oxford, United Kingdom.
Michael A McDonoughDepartment of Chemistry, University of Oxford, Oxford, United Kingdom.ORCID 0000-0003-4664-6942
Somdutta DhirSir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.ORCID 0000-0003-1987-3971
Nick J ProudfootSir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.ORCID 0000-0001-8646-3222
Christopher J SchofieldDepartment of Chemistry, University of Oxford, Oxford, United Kingdom.ORCID 0000-0002-0290-6565
University of Oxford · GBUniversity of Birmingham · GB

Funding

Biotechnology and Biological Sciences Research CouncilCancer Research UKEuropean Research Council 339270Medical Research Council MR/L007665/1Wellcome TrustWellcome Trust 105045/Z/14/ZWellcome Trust 107928/Z/15/ZWellcome Trust Sir Henry Dale Fellowship 200473/Z/16/Z
6 · The paper itself

Abstract

Replication-dependent (RD) core histone mRNA produced during S-phase is the only known metazoan protein-coding mRNA presenting a 3' stem-loop instead of the otherwise universal polyA tail. A metallo β-lactamase (MBL) fold enzyme, cleavage and polyadenylation specificity factor 73 (CPSF73), is proposed to be the sole endonuclease responsible for 3' end processing of both mRNA classes. We report cellular, genetic, biochemical, substrate selectivity, and crystallographic studies providing evidence that an additional endoribonuclease, MBL domain containing protein 1 (MBLAC1), is selective for 3' processing of RD histone pre-mRNA during the S-phase of the cell cycle. Depletion of MBLAC1 in cells significantly affects cell cycle progression thus identifying MBLAC1 as a new type of S-phase-specific cancer target.

Indexed as

Amino Acid Sequencebeta-LactamasesBinding SitesCloning, MolecularCrystallography, X-RayEndoribonucleasesEscherichia coliGene ExpressionGenetic VectorsHEK293 CellsHeLa CellsHistonesHumansHydrolasesKineticsModels, Molecularbeta-LactamasesEndoribonucleasesHistonesHydrolasesLACTB2 protein, humanMBLAC1 protein, humanRecombinant ProteinsRNA, MessengerRNase Zcell biologychromosomesendoribonucleasegene expressionhistone pre-mRNA 3' end processinghumanMBL domain containing protein 1metallo β-lactamaseS-phase

Identifiers

PMID30507380
PMCPMC6303110
OpenAlexW2902919834

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.