Evidence map›Paper›PMID 34407997›Full record

ArticleLife science alliance2021

A role for Rad5 in ribonucleoside monophosphate (rNMP) tolerance.

Menattallah Elserafy, Iman El-Shiekh, Dalia Fleifel, Reham Atteya, Abdelrahman AlOkda, Mohamed M Abdrabbou, Mostafa Nasr, Sherif F El-Khamisy

Open access · goldAbstract read
In one paragraph

Article in Life science alliance, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 51% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. 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 2 countries.

Menattallah ElserafyCenter for Genomics, Helmy Institute for Medical Sciences, Zewail City of Science and Technology, Giza, Egypt.ORCID 0000-0002-0272-8498
Iman El-ShiekhCenter for Genomics, Helmy Institute for Medical Sciences, Zewail City of Science and Technology, Giza, Egypt.ORCID 0000-0003-4828-2310
Dalia FleifelCenter for Genomics, Helmy Institute for Medical Sciences, Zewail City of Science and Technology, Giza, Egypt.
Reham AtteyaCenter for Genomics, Helmy Institute for Medical Sciences, Zewail City of Science and Technology, Giza, Egypt.ORCID 0000-0002-3260-6723
Abdelrahman AlOkdaCenter for Genomics, Helmy Institute for Medical Sciences, Zewail City of Science and Technology, Giza, Egypt.ORCID 0000-0002-0352-7292
Mohamed M AbdrabbouCenter for Genomics, Helmy Institute for Medical Sciences, Zewail City of Science and Technology, Giza, Egypt.ORCID 0000-0003-2778-7483
Mostafa NasrCenter for Genomics, Helmy Institute for Medical Sciences, Zewail City of Science and Technology, Giza, Egypt.
Sherif F El-KhamisyCenter for Genomics, Helmy Institute for Medical Sciences, Zewail City of Science and Technology, Giza, Egypt S.el-khamisy@sheffield.ac.uk.ORCID 0000-0003-2721-7763
Zewail City of Science and Technology · EGUniversity of Bradford · GB

Funding

Wellcome Trust 103844
6 · The paper itself

Abstract

Ribonucleoside monophosphate (rNMP) incorporation in genomic DNA poses a significant threat to genomic integrity. In addition to repair, DNA damage tolerance mechanisms ensure replication progression upon encountering unrepaired lesions. One player in the tolerance mechanism is Rad5, which is an E3 ubiquitin ligase and helicase. Here, we report a new role for yeast Rad5 in tolerating rNMP incorporation, in the absence of the bona fide ribonucleotide excision repair pathway via RNase H2. This role of Rad5 is further highlighted after replication stress induced by hydroxyurea or by increasing rNMP genomic burden using a mutant DNA polymerase (Pol ε - Pol2-M644G). We further demonstrate the importance of the ATPase and ubiquitin ligase domains of Rad5 in rNMP tolerance. These findings suggest a similar role for the human Rad5 homologues helicase-like transcription factor (HLTF) and SNF2 Histone Linker PHD RING Helicase (SHPRH) in rNMP tolerance, which may impact the response of cancer cells to replication stress-inducing therapeutics.

Indexed as

Adenosine TriphosphatasesCell Cycle CheckpointsDNA DamageDNA HelicasesGenomicsMutationProtein BindingProtein Interaction Domains and MotifsRibonucleotidesStress, PhysiologicalUbiquitin-Protein Ligase ComplexesYeastsAdenosine TriphosphatasesDNA HelicasesRibonucleotidesUbiquitin-Protein Ligase Complexes

Identifiers

PMID34407997
PMCPMC8380674
OpenAlexW3195513001

What Socratic 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 Socratic graph.