Evidence map›Paper›PMID 28160602›Full record

ArticleNucleic acids research2017

Regulation of telomere metabolism by the RNA processing protein Xrn1.

Daniele Cesena, Corinne Cassani, Emanuela Rizzo, Michael Lisby, Diego Bonetti, Maria Pia Longhese

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Structure of the 80S ribosome-Xrn1 nuclease complex.Nature structural & molecular biology · 2019
    Article
  5. 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 2 countries.

Daniele CesenaDipartimento di Biotecnologie e Bioscienze, Università di Milano-Bicocca, Milan 20126, Italy.
Corinne CassaniDipartimento di Biotecnologie e Bioscienze, Università di Milano-Bicocca, Milan 20126, Italy.
Emanuela RizzoDipartimento di Biotecnologie e Bioscienze, Università di Milano-Bicocca, Milan 20126, Italy.
Michael LisbyDepartment of Biology, University of Copenhagen, DK-2200 Copenhagen N, Denmark.
Diego BonettiDipartimento di Biotecnologie e Bioscienze, Università di Milano-Bicocca, Milan 20126, Italy.
Maria Pia LongheseDipartimento di Biotecnologie e Bioscienze, Università di Milano-Bicocca, Milan 20126, Italy.
University of Milano-Bicocca · ITUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Telomeric DNA consists of repetitive G-rich sequences that terminate with a 3΄-ended single stranded overhang (G-tail), which is important for telomere extension by telomerase. Several proteins, including the CST complex, are necessary to maintain telomere structure and length in both yeast and mammals. Emerging evidence indicates that RNA processing factors play critical, yet poorly understood, roles in telomere metabolism. Here, we show that the lack of the RNA processing proteins Xrn1 or Rrp6 partially bypasses the requirement for the CST component Cdc13 in telomere protection by attenuating the activation of the DNA damage checkpoint. Xrn1 is necessary for checkpoint activation upon telomere uncapping because it promotes the generation of single-stranded DNA. Moreover, Xrn1 maintains telomere length by promoting the association of Cdc13 to telomeres independently of ssDNA generation and exerts this function by downregulating the transcript encoding the telomerase inhibitor Rif1. These findings reveal novel roles for RNA processing proteins in the regulation of telomere metabolism with implications for genome stability in eukaryotes.

Indexed as

Telomere HomeostasisDNA, Single-StrandedExoribonucleasesExosome Multienzyme Ribonuclease ComplexMutationRepressor ProteinsRNA Processing, Post-TranscriptionalSaccharomyces cerevisiae ProteinsTelomereTelomere-Binding ProteinsTemperatureCdc13 protein, S cerevisiaeDNA, Single-StrandedExoribonucleasesExosome Multienzyme Ribonuclease ComplexRepressor ProteinsRIF1 protein, S cerevisiaeRRP6 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTelomere-Binding ProteinsXRN1 protein, S cerevisiae

Identifiers

PMID28160602
PMCPMC5397203
OpenAlexW2583108679

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.