Evidence map›Paper›PMID 25114049›Full record

ArticleNucleic acids research2014

Structure and function of TatD exonuclease in DNA repair.

Yi-Chen Chen, Chia-Lung Li, Yu-Yuan Hsiao, Yulander Duh, Hanna S Yuan

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
0.4field-weighted citation impact, top 35% 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

28 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Cellular Responses to Widespread DNA Replication Stress.International journal of molecular sciences · 2023
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Molecular Basis for Luteolin as a Natural TatD DNase Inhibitor inInternational journal of molecular sciences · 2022
    Article
  17. Proteomics and transcriptomic analysis ofCurrent research in microbial sciences · 2021
    Article
  18. Article
  19. Article
  20. 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

5 authors at 3 institutions in 1 country.

Yi-Chen ChenInstitute of Molecular Biology, Academia Sinica, Taipei 11529, Taiwan, ROC.
Chia-Lung LiInstitute of Molecular Biology, Academia Sinica, Taipei 11529, Taiwan, ROC.
Yu-Yuan HsiaoDepartment of Biological Science and Technology, National Chiao Tung University, Hsinchu 30068, Taiwan, ROC.
Yulander DuhInstitute of Molecular Biology, Academia Sinica, Taipei 11529, Taiwan, ROC.
Hanna S YuanInstitute of Molecular Biology, Academia Sinica, Taipei 11529, Taiwan, ROC Graduate Institute of Biochemistry and Molecular Biology, College of Medicine, National Taiwan University, Taipei 10048, Taiwan, ROC hanna@sinica.edu.tw.
Institute of Molecular Biology, Academia Sinica · TWNational Taiwan University · TWNational Yang Ming Chiao Tung University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TatD is an evolutionarily conserved protein with thousands of homologues in all kingdoms of life. It has been suggested that TatD participates in DNA fragmentation during apoptosis in eukaryotic cells. However, the cellular functions and biochemical properties of TatD in bacterial and non-apoptotic eukaryotic cells remain elusive. Here we show that Escherichia coli TatD is a Mg(2+)-dependent 3'-5' exonuclease that prefers to digest single-stranded DNA and RNA. TatD-knockout cells are less resistant to the DNA damaging agent hydrogen peroxide, and TatD can remove damaged deaminated nucleotides from a DNA chain, suggesting that it may play a role in the H2O2-induced DNA repair. The crystal structure of the apo-form TatD and TatD bound to a single-stranded three-nucleotide DNA was determined by X-ray diffraction methods at a resolution of 2.0 and 2.9 Å, respectively. TatD has a TIM-barrel fold and the single-stranded DNA is bound at the loop region on the top of the barrel. Mutational studies further identify important conserved metal ion-binding and catalytic residues in the TatD active site for DNA hydrolysis. We thus conclude that TatD is a new class of TIM-barrel 3'-5' exonuclease that not only degrades chromosomal DNA during apoptosis but also processes single-stranded DNA during DNA repair.

Indexed as

DNA RepairCatalytic DomainDNADNA Repair EnzymesEscherichia coliEscherichia coli ProteinsExodeoxyribonucleasesExonucleasesMagnesiumModels, MolecularRNASequence AlignmentDNADNA Repair EnzymesEscherichia coli ProteinsExodeoxyribonucleasesExonucleasesMagnesiumRNATatD protein, E coli

Identifiers

PMID25114049
PMCPMC4176340
OpenAlexW2172256428

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.