Evidence map›Paper›PMID 9501103›Full record

ArticleThe EMBO journal1998

Components of the Ku-dependent non-homologous end-joining pathway are involved in telomeric length maintenance and telomeric silencing.

S J Boulton, S P Jackson

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 269 papers.

0numbers the graph read from it
0cells of the map it votes in
269citing papers in PubMed
21.5field-weighted citation impact, top 1% 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

269 citing papers in PubMed, 636 citations in OpenAlex.

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209 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

S J BoultonWellcome/CRC Institute, Tennis Court Road, Cambridge CB2 1QR, UK.
S P Jackson
University of Cambridge · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

In the budding yeast, Saccharomyces cerevisiae, genes in close proximity to telomeres are subject to transcriptional silencing through the process of telomere position effect (TPE). Here, we show that the protein Ku, previously implicated in DNA double-strand break (DSB) repair and in telomeric length maintenance, is also essential for telomeric silencing. Furthermore, using an in vivo plasmid rejoining assay, we demonstrate that SIR2, SIR3 and SIR4, three genes shown previously to function in TPE, are essential for Ku-dependent DSB repair. As is the case for Ku-deficient strains, residual repair operating in the absence of the SIR gene products ensues through an error-prone DNA repair pathway that results in terminal deletions. To identify novel components of the Ku-associated DSB repair pathway, we have tested several other candidate genes for their involvement in DNA DSB repair, telomeric maintenance and TPE. We show that TEL1, a gene required for telomeric length maintenance, is not required for either DNA DSB repair or TPE. However, RAD50, MRE11 and XRS2 function both in Ku-dependent DNA DSB repair and in telomeric length maintenance, although they have no major effects on TPE. These data provide important insights into DNA DSB repair and the linkage of this process to telomere length homeostasis and transcriptional silencing.

Indexed as

Antigens, NuclearDNA HelicasesEndodeoxyribonucleasesExodeoxyribonucleasesHistone DeacetylasesSaccharomyces cerevisiae ProteinsSilent Information Regulator Proteins, Saccharomyces cerevisiaeDNA-Binding ProteinsDNA RepairFungal ProteinsGenes, FungalGenetic MarkersKu AutoantigenMutagenesis, InsertionalNuclear ProteinsSaccharomyces cerevisiaeAntigens, NuclearDNA-Binding ProteinsDNA HelicasesEndodeoxyribonucleasesExodeoxyribonucleasesFungal ProteinsGenetic Markershigh affinity DNA-binding factor, S cerevisiaeHistone DeacetylasesKu AutoantigenMRE11 protein, S cerevisiaeNuclear ProteinsRAD50 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSilent Information Regulator Proteins, Saccharomyces cerevisiaeSIR1 protein, S cerevisiaeSIR2 protein, S cerevisiaeSIR3 protein, S cerevisiaeSIR4 protein, S cerevisiaeSIRT1 protein, humanSirtuin 1Sirtuin 2SirtuinsTrans-ActivatorsXRCC5 protein, humanXrcc6 protein, humanXRS2 protein, S cerevisiae

Identifiers

PMID9501103
PMCPMC1170529
OpenAlexW2157451489

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.