Evidence map›Paper›PMID 39174552›Full record

ArticleNature communications2024

Sae2 controls Mre11 endo- and exonuclease activities by different mechanisms.

Tomoki Tamai, Giordano Reginato, Ryusei Ojiri, Issei Morita, Alexandra Avrutis, Petr Cejka, Miki Shinohara, Katsunori Sugimoto

Abstract read
In one paragraph

Article in Nature communications, 2024. 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.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. 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.

Tomoki Tamai *Faculty of Advanced Bioscience, Graduate School of Agriculture, Kindai University, Nara City, Nara, 631-8505, Japan.
Giordano Reginato *Faculty of Biomedical Sciences, Institute for Research in Biomedicine, Università della Svizzera italiana (USI), 6500, Bellinzona, Switzerland.ORCID 0009-0002-5284-4339
Ryusei OjiriFaculty of Advanced Bioscience, Graduate School of Agriculture, Kindai University, Nara City, Nara, 631-8505, Japan.
Issei MoritaFaculty of Advanced Bioscience, Graduate School of Agriculture, Kindai University, Nara City, Nara, 631-8505, Japan.
Alexandra AvrutisDepartment of Microbiology, Biochemistry and Molecular Genetics, New Jersey Medical School, Rutgers, the State University of New Jersey, Newark, NJ, 07103, USA.
Petr CejkaFaculty of Biomedical Sciences, Institute for Research in Biomedicine, Università della Svizzera italiana (USI), 6500, Bellinzona, Switzerland. petr.cejka@irb.usi.ch.ORCID 0000-0002-9087-032X
Miki ShinoharaFaculty of Advanced Bioscience, Graduate School of Agriculture, Kindai University, Nara City, Nara, 631-8505, Japan. mikis@nara.kindai.ac.jp.ORCID 0000-0002-7413-8235
Katsunori SugimotoDepartment of Microbiology, Biochemistry and Molecular Genetics, New Jersey Medical School, Rutgers, the State University of New Jersey, Newark, NJ, 07103, USA. nori.sugimoto@rutgers.edu.ORCID 0000-0001-9374-2190

Funding

Regulation of ATM- and ATR-related protein kinasesR01GM120730 · NIGMS · RBHS-NEW JERSEY MEDICAL SCHOOL · PI SUGIMOTO, KATSUNORI · 2016 to 2017
$636k
NIGMS NIH HHS R01 GM120730Swiss National Science FoundationU.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R01GM120730
6 · The paper itself

Abstract

DNA double-strand breaks (DSBs) must be repaired to ensure cell survival and genomic integrity. In yeast, the Mre11-Rad50-Xrs2 complex (MRX) collaborates with Sae2 to initiate DSB repair. Sae2 stimulates two MRX nuclease activities, endonuclease and 3'-5' exonuclease. However, how Sae2 controls the two nuclease activities remains enigmatic. Using a combined genetic and biochemical approach, we identified a separation-of-function rad50 mutation, rad50-C47, that causes a defect in Sae2-dependent MRX 3'-5' exonuclease activity, but not endonuclease activity. We found that both the endo- and 3'-5' exonuclease activities are essential to release Spo11 from DNA ends, whereas only the endonuclease activity is required for hairpin removal. We also uncovered that MRX-Sae2 endonuclease introduces a cleavage at defined distances from the Spo11-blocked end with gradually decreasing efficiency. Our findings demonstrate that Sae2 stimulates the MRX endo- and exonuclease activities via Rad50 by different mechanisms, ensuring diverse actions of MRX-Sae2 nuclease at DNA ends.

Indexed as

DNA-Binding ProteinsDNA Breaks, Double-StrandedEndodeoxyribonucleasesEndonucleasesExodeoxyribonucleasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA, FungalDNA RepairMeiotic Recombination Protein SPO11MutationDNA-Binding ProteinsDNA, FungalEndodeoxyribonucleasesEndonucleasesExodeoxyribonucleasesMeiotic Recombination Protein SPO11MRE11 protein, S cerevisiaeRAD50 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSAE2 protein, S cerevisiaeSpo11 protein, S cerevisiaeXRS2 protein, S cerevisiae

Identifiers

PMID39174552
PMCPMC11341764

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.