Evidence map›Paper›PMID 28604726›Full record

ArticleNature structural & molecular biology2017

Rif1 maintains telomeres and mediates DNA repair by encasing DNA ends.

Stefano Mattarocci, Julia K Reinert, Richard D Bunker, Gabriele A Fontana, Tianlai Shi, Dominique Klein, Simone Cavadini, Mahamadou Faty, Maksym Shyian, Lukas Hafner and 3 more

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

31 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
  2. Repetitive Sequence Stability in Embryonic Stem Cells.International journal of molecular sciences · 2024
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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

13 authors at 3 institutions in 1 country.

Stefano MattarocciDepartment of Molecular Biology and Institute of Genetics and Genomics in Geneva (iGE3), University of Geneva, Geneva, Switzerland.
Julia K ReinertFriedrich Miescher Institute for Biomedical Research, Basel, Switzerland.
Richard D BunkerFriedrich Miescher Institute for Biomedical Research, Basel, Switzerland.
Gabriele A FontanaFriedrich Miescher Institute for Biomedical Research, Basel, Switzerland.
Tianlai ShiFriedrich Miescher Institute for Biomedical Research, Basel, Switzerland.
Dominique KleinFriedrich Miescher Institute for Biomedical Research, Basel, Switzerland.
Simone CavadiniFriedrich Miescher Institute for Biomedical Research, Basel, Switzerland.
Mahamadou FatyFriedrich Miescher Institute for Biomedical Research, Basel, Switzerland.
Maksym ShyianDepartment of Molecular Biology and Institute of Genetics and Genomics in Geneva (iGE3), University of Geneva, Geneva, Switzerland.
Lukas HafnerDepartment of Molecular Biology and Institute of Genetics and Genomics in Geneva (iGE3), University of Geneva, Geneva, Switzerland.
David ShoreDepartment of Molecular Biology and Institute of Genetics and Genomics in Geneva (iGE3), University of Geneva, Geneva, Switzerland.ORCID http://orcid.org/0000-0002-9859-143X
Nicolas H ThomäFriedrich Miescher Institute for Biomedical Research, Basel, Switzerland.
Ulrich RassFriedrich Miescher Institute for Biomedical Research, Basel, Switzerland.ORCID http://orcid.org/0000-0001-9275-9062
Friedrich Miescher Institute · CHUniversity of Geneva · CHUniversity of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In yeast, Rif1 is part of the telosome, where it inhibits telomerase and checkpoint signaling at chromosome ends. In mammalian cells, Rif1 is not telomeric, but it suppresses DNA end resection at chromosomal breaks, promoting repair by nonhomologous end joining (NHEJ). Here, we describe crystal structures for the uncharacterized and conserved ∼125-kDa N-terminal domain of Rif1 from Saccharomyces cerevisiae (Rif1-NTD), revealing an α-helical fold shaped like a shepherd's crook. We identify a high-affinity DNA-binding site in the Rif1-NTD that fully encases DNA as a head-to-tail dimer. Engagement of the Rif1-NTD with telomeres proved essential for checkpoint control and telomere length regulation. Unexpectedly, Rif1-NTD also promoted NHEJ at DNA breaks in yeast, revealing a conserved role of Rif1 in DNA repair. We propose that tight associations between the Rif1-NTD and DNA gate access of processing factors to DNA ends, enabling Rif1 to mediate diverse telomere maintenance and DNA repair functions.

Indexed as

DNA End-Joining RepairBinding SitesCrystallography, X-RayDNADNA-Binding ProteinsModels, MolecularProtein BindingProtein ConformationProtein MultimerizationRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTelomereTelomere-Binding ProteinsDNADNA-Binding ProteinsRepressor ProteinsRIF1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTelomere-Binding Proteins

Identifiers

PMID28604726
OpenAlexW2625599791

What OpenQuestion holds

Textmetadata
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.