Evidence map›Paper›PMID 16314503›Full record

ArticleMolecular and cellular biology2005

Mutations of the Yku80 C terminus and Xrs2 FHA domain specifically block yeast nonhomologous end joining.

Phillip L Palmbos, James M Daley, Thomas E Wilson

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

44 citing papers in PubMed, 78 citations in OpenAlex.

  1. Rap1-mediated steric hindrance protects telomeres from MRX sensing.Nature structural & molecular biology · 2026
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  14. Consider the workhorse: Nonhomologous end-joining in budding yeast.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2016
    Review
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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

3 authors at 1 institution in 1 country.

Phillip L PalmbosDepartment of Pathology, University of Michigan Medical School, Ann Arbor, 48109-0602, USA.
James M Daley
Thomas E Wilson
University of Michigan–Ann Arbor · US

Funding

CELLULAR AND MOLECULAR BIOLOGY AT MICHIGANT32GM007315 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PUTHENVEEDU, MANOJKUMAR A · 1985 to 2021
$12.8M
Systematic Genetic Analysis of Yeast NHEJR01CA102563 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WILSON, THOMAS EDWARD · 2004 to 2014
$2.4M
End Processing in DNA Double Strand Break RepairR01CA090911 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WILSON, THOMAS EDWARD · 2001 to 2004
$884k
NCI NIH HHS R01 CA090911NCI NIH HHS R01 CA102563NCI NIH HHS R01CA102563NIGMS NIH HHS T32 GM007315
6 · The paper itself

Abstract

The nonhomologous end-joining (NHEJ) pathway of DNA double-strand break repair requires three protein complexes in Saccharomyces cerevisiae: MRX (Mre11-Rad50-Xrs2), Ku (Ku70-Ku80), and DNA ligase IV (Dnl4-Lif1-Nej1). Much is known about the interactions that mediate the formation of each complex, but little is known about how they act together during repair. A comprehensive yeast two-hybrid screen of the NHEJ factors of S. cerevisiae revealed all known interactions within the MRX, Ku, and DNA ligase IV complexes, as well as three additional, weaker interactions between Yku80-Dnl4, Xrs2-Lif1, and Mre11-Yku80. Individual and combined deletions of the Yku80 C terminus and the Xrs2 forkhead-associated (FHA) domain were designed based on the latter two-hybrid results. These deletions synergistically blocked NHEJ but not the telomere and recombination functions of Ku and MRX, confirming that these protein regions are functionally important specifically for NHEJ. Further mutational analysis of Yku80 identified a putative C-terminal amphipathic alpha-helix that is both required for its NHEJ function and strikingly similar to a DNA-dependent protein kinase interaction motif in human Ku80. These results identify a novel role in yeast NHEJ for the poorly characterized Ku80 C-terminal and Xrs2 FHA domains, and they suggest that redundant binding of DNA ligase IV facilitates completion of this DNA repair event.

Indexed as

Antigens, NuclearDNA-Binding ProteinsDNA DamageDNA, FungalDNA Ligase ATPDNA LigasesDNA Mutational AnalysisDNA RepairEndodeoxyribonucleasesExodeoxyribonucleasesKu AutoantigenMolecular Sequence DataMutationProtein Structure, SecondaryProtein Structure, TertiaryRecombination, GeneticAntigens, NuclearDNA-Binding ProteinsDNA, FungalDNA Ligase ATPDNA LigasesDNL4 protein, S cerevisiaeEndodeoxyribonucleasesExodeoxyribonucleaseshigh affinity DNA-binding factor, S cerevisiaeKu AutoantigenLIG4 protein, humanMRE11 protein, S cerevisiaeRAD50 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsXrcc6 protein, humanXRS2 protein, S cerevisiaeYKU80 protein, S cerevisiae

Identifiers

PMID16314503
PMCPMC1316971
OpenAlexW2098813501

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.