Evidence map›Paper›PMID 21149442›Full record

ArticleThe Journal of biological chemistry2011

Yeast Nej1 is a key participant in the initial end binding and final ligation steps of nonhomologous end joining.

Xi Chen, Alan E Tomkinson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. 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
1.2field-weighted citation impact, top 22% 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, 50 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. International journal of molecular sciences · 2022
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. The Multifaceted Roles of Ku70/80.International journal of molecular sciences · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Consider the workhorse: Nonhomologous end-joining in budding yeast.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2016
    Review
  19. Article
  20. Regulation of recombination and genomic maintenance.Cold Spring Harbor perspectives in biology · 2015
    Review
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.

Xi ChenRadiation Oncology Research Laboratory, Department of Radiation Oncology, and The Marlene and Stewart Greenebaum Cancer Center, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA.
Alan E Tomkinson
University of Maryland Marlene and Stewart Greenebaum Comprehensive Cancer Center

Funding

CELLULAR FUNCTIONS OF EUKARYOTIC LIGASESR01GM047251 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI DAVIS, ANTHONY J, TOMKINSON, ALAN E · 1998 to 2021
$4.7M
CELLULAR FUNCTIONS OF EUKARYOTIC DNA LIGASESR29GM047251 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI TOMKINSON, ALAN E · 1993 to 1997
–
NIGMS NIH HHS GM47251NIGMS NIH HHS R01 GM047251
6 · The paper itself

Abstract

In Saccharomyces cerevisiae, the key components of the nonhomologous end joining (NHEJ) pathway that repairs DNA double-strand breaks (DSBs) are yeast Ku (yKu), Mre11-Rad50-Xrs2, Dnl4-Lif1, and Nej1. Here, we examined the role of Nej1 in NHEJ by a combination of molecular genetic and biochemical approaches. As expected, the recruitment of Nej1 to in vivo DSBs is dependent upon yKu. Surprisingly, Nej1 is required for the stable binding of yKu to in vivo DSBs, in addition to Dnl4-Lif1. Thus, Nej1 and Dnl4-Lif1 are independently recruited by yKu to in vivo DSBs, forming a stable ternary complex that channels DSBs into the NHEJ pathway. In accord with these results, purified Nej1 interacts with yKu and preferentially binds to DNA ends bound by yKu. Furthermore, the binding of a mixture of Nej1 and Dnl4-Lif1 to DNA ends bound by yKu is greater than the sum of the binding of the individual proteins, indicating that pairwise interactions among yKu, Nej1, and Dnl4-Lif1 contribute to complex assembly at DNA ends. Nej1 stimulates intermolecular ligation by Dnl4-Lif1, but, more interestingly, the addition of Nej1 results in more than one intermolecular ligation per Dnl4 molecule. Thus, Nej1 not only plays an important role in determining repair pathway choice by participating in the initial NHEJ complex formed at DSBs but also contributes to the reactivation of Dnl4-Lif1 after repair is complete, thereby increasing the capacity of the NHEJ repair pathway.

Indexed as

DNA Breaks, Double-StrandedDNA-Binding ProteinsDNA, FungalDNA Ligase ATPDNA LigasesDNA RepairMultiprotein ComplexesProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA-Binding ProteinsDNA, FungalDNA Ligase ATPDNA LigasesLIF1 protein, S cerevisiaeMultiprotein ComplexesNEJ1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsYKU70 protein, S cerevisiae

Identifiers

PMID21149442
PMCPMC3039407
OpenAlexW2068161156

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.