Evidence map›Paper›PMID 31410466›Full record

ArticleNucleic acids research2019

Structure and DNA damage-dependent derepression mechanism for the XRE family member DG-DdrO.

Huizhi Lu, Liangyan Wang, Shengjie Li, Chaoming Pan, Kaiying Cheng, Yuxia Luo, Hong Xu, Bing Tian, Ye Zhao, Yuejin Hua

Abstract read
In one paragraph

Article in Nucleic acids research, 2019. 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
–field-weighted citation impact
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.

  1. Review
  2. Radiation-response inFEMS microbes · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Bacterial PprI-DdrO system evolved from ImmA-ImmR system in the prophage.Protein science : a publication of the Protein Society · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
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  19. The potential of native and engineered Clostridia for biomass biorefining.Frontiers in bioengineering and biotechnology · 2024
    Review
  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

10 authors.

Huizhi LuMOE Key Laboratory of Biosystems Homeostasis & Protection, Zhejiang University, China.
Liangyan WangMOE Key Laboratory of Biosystems Homeostasis & Protection, Zhejiang University, China.
Shengjie LiMOE Key Laboratory of Biosystems Homeostasis & Protection, Zhejiang University, China.
Chaoming PanMOE Key Laboratory of Biosystems Homeostasis & Protection, Zhejiang University, China.
Kaiying ChengMOE Key Laboratory of Biosystems Homeostasis & Protection, Zhejiang University, China.
Yuxia LuoMOE Key Laboratory of Biosystems Homeostasis & Protection, Zhejiang University, China.
Hong XuMOE Key Laboratory of Biosystems Homeostasis & Protection, Zhejiang University, China.
Bing TianMOE Key Laboratory of Biosystems Homeostasis & Protection, Zhejiang University, China.
Ye ZhaoMOE Key Laboratory of Biosystems Homeostasis & Protection, Zhejiang University, China.
Yuejin HuaMOE Key Laboratory of Biosystems Homeostasis & Protection, Zhejiang University, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DdrO is an XRE family transcription repressor that, in coordination with the metalloprotease PprI, is critical in the DNA damage response of Deinococcus species. Here, we report the crystal structure of Deinococcus geothermalis DdrO. Biochemical and structural studies revealed the conserved recognizing α-helix and extended dimeric interaction of the DdrO protein, which are essential for promoter DNA binding. Two conserved oppositely charged residues in the HTH motif of XRE family proteins form salt bridge interactions that are essential for promoter DNA binding. Notably, the C-terminal domain is stabilized by hydrophobic interactions of leucine/isoleucine-rich helices, which is critical for DdrO dimerization. Our findings suggest that DdrO is a novel XRE family transcriptional regulator that forms a distinctive dimer. The structure also provides insight into the mechanism of DdrO-PprI-mediated DNA damage response in Deinococcus.

Indexed as

Amino Acid SequenceBacterial ProteinsDeinococcusDNA DamageGene Expression Regulation, BacterialHelix-Turn-Helix MotifsMetalloproteasesPromoter Regions, GeneticProtein BindingProtein Structure, SecondaryTranscription FactorsBacterial ProteinsMetalloproteasesTranscription Factors

Identifiers

PMID31410466
PMCPMC6765133

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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.