Evidence map›Paper›PMID 28432356›Full record

ArticleScientific reports2017

A role of human RNase P subunits, Rpp29 and Rpp21, in homology directed-repair of double-strand breaks.

Enas R Abu-Zhayia, Hanan Khoury-Haddad, Noga Guttmann-Raviv, Raphael Serruya, Nayef Jarrous, Nabieh Ayoub

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

18 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. RNase P: Beyond Precursor tRNA Processing.Genomics, proteomics & bioinformatics · 2024
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. The infinite possibilities of RNA therapeutics.Journal of industrial microbiology & biotechnology · 2021
    Article
  11. Article
  12. The Dynamic Network of RNP RNase P Subunits.International journal of molecular sciences · 2021
    Review
  13. Article
  14. Genetics and the heart rate response to exercise.Cellular and molecular life sciences : CMLS · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. 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

6 authors at 2 institutions in 1 country.

Enas R Abu-ZhayiaDepartment of Biology, Technion - Israel Institute of Technology, Haifa, 3200003, Israel.
Hanan Khoury-HaddadDepartment of Biology, Technion - Israel Institute of Technology, Haifa, 3200003, Israel.
Noga Guttmann-RavivDepartment of Biology, Technion - Israel Institute of Technology, Haifa, 3200003, Israel.
Raphael SerruyaDepartment of Microbiology and Molecular Genetics, IMRIC, The Hebrew University-Hadassah Medical School, 91120, Jerusalem, Israel.
Nayef JarrousDepartment of Microbiology and Molecular Genetics, IMRIC, The Hebrew University-Hadassah Medical School, 91120, Jerusalem, Israel. jarrous@md.huji.ac.il.
Nabieh AyoubDepartment of Biology, Technion - Israel Institute of Technology, Haifa, 3200003, Israel. ayoubn@technion.ac.il.
Technion – Israel Institute of Technology · ILHebrew University of Jerusalem · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA damage response (DDR) is needed to repair damaged DNA for genomic integrity preservation. Defective DDR causes accumulation of deleterious mutations and DNA lesions that can lead to genomic instabilities and carcinogenesis. Identifying new players in the DDR, therefore, is essential to advance the understanding of the molecular mechanisms by which cells keep their genetic material intact. Here, we show that the core protein subunits Rpp29 and Rpp21 of human RNase P complex are implicated in DDR. We demonstrate that Rpp29 and Rpp21 depletion impairs double-strand break (DSB) repair by homology-directed repair (HDR), but has no deleterious effect on the integrity of non-homologous end joining. We also demonstrate that Rpp29 and Rpp21, but not Rpp14, Rpp25 and Rpp38, are rapidly and transiently recruited to laser-microirradiated sites. Rpp29 and Rpp21 bind poly ADP-ribose moieties and are recruited to DNA damage sites in a PARP1-dependent manner. Remarkably, depletion of the catalytic H1 RNA subunit diminishes their recruitment to laser-microirradiated regions. Moreover, RNase P activity is augmented after DNA damage in a PARP1-dependent manner. Altogether, our results describe a previously unrecognized function of the RNase P subunits, Rpp29 and Rpp21, in fine-tuning HDR of DSBs.

Indexed as

Recombinational DNA RepairCell LineDNADNA Breaks, Double-StrandedDNA End-Joining RepairHumansPoly-ADP-Ribose Binding ProteinsPoly (ADP-Ribose) Polymerase-1Ribonuclease PRibonucleasesRibonucleoproteinsDNAPARP1 protein, humanPoly-ADP-Ribose Binding ProteinsPoly (ADP-Ribose) Polymerase-1POP4 protein, humanRibonuclease PRibonucleasesRibonucleoproteinsRPP21 protein, human

Identifiers

PMID28432356
PMCPMC5430778
OpenAlexW2605416909

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Registered trials

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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.