Evidence map›Paper›PMID 38424107›Full record

ArticleNature communications2024

The Deinococcus protease PprI senses DNA damage by directly interacting with single-stranded DNA.

Huizhi Lu, Zijing Chen, Teng Xie, Shitong Zhong, Shasha Suo, Shuang Song, Liangyan Wang, Hong Xu, Bing Tian, Ye Zhao and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

18 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
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  6. Article
  7. Radiation-response inFEMS microbes · 2026
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Bacterial PprI-DdrO system evolved from ImmA-ImmR system in the prophage.Protein science : a publication of the Protein Society · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

12 authors at 3 institutions in 3 countries.

Huizhi Lu *MOE Key Laboratory of Biosystems Homeostasis & Protection, Institute of Biophysics, College of Life Sciences, Zhejiang University, Hangzhou, China.ORCID 0000-0002-2408-4427
Zijing Chen *MOE Key Laboratory of Biosystems Homeostasis & Protection, Institute of Biophysics, College of Life Sciences, Zhejiang University, Hangzhou, China.
Teng XieMOE Key Laboratory of Biosystems Homeostasis & Protection, Institute of Biophysics, College of Life Sciences, Zhejiang University, Hangzhou, China.
Shitong ZhongMOE Key Laboratory of Biosystems Homeostasis & Protection, Institute of Biophysics, College of Life Sciences, Zhejiang University, Hangzhou, China.
Shasha SuoMOE Key Laboratory of Biosystems Homeostasis & Protection, Institute of Biophysics, College of Life Sciences, Zhejiang University, Hangzhou, China.
Shuang SongMOE Key Laboratory of Biosystems Homeostasis & Protection, Institute of Biophysics, College of Life Sciences, Zhejiang University, Hangzhou, China.ORCID 0000-0003-4075-2226
Liangyan WangMOE Key Laboratory of Biosystems Homeostasis & Protection, Institute of Biophysics, College of Life Sciences, Zhejiang University, Hangzhou, China.
Hong XuMOE Key Laboratory of Biosystems Homeostasis & Protection, Institute of Biophysics, College of Life Sciences, Zhejiang University, Hangzhou, China.
Bing TianMOE Key Laboratory of Biosystems Homeostasis & Protection, Institute of Biophysics, College of Life Sciences, Zhejiang University, Hangzhou, China.ORCID 0000-0002-9533-6409
Ye ZhaoMOE Key Laboratory of Biosystems Homeostasis & Protection, Institute of Biophysics, College of Life Sciences, Zhejiang University, Hangzhou, China. yezhao@zju.edu.cn.ORCID 0000-0002-5455-2586
Ruhong ZhouMOE Key Laboratory of Biosystems Homeostasis & Protection, Institute of Biophysics, College of Life Sciences, Zhejiang University, Hangzhou, China. rhzhou@zju.edu.cn.ORCID 0000-0001-8624-5591
Yuejin HuaMOE Key Laboratory of Biosystems Homeostasis & Protection, Institute of Biophysics, College of Life Sciences, Zhejiang University, Hangzhou, China. yjhua@zju.edu.cn.ORCID 0000-0001-6743-0919
Institute of Biophysics · CNZhejiang Cancer Hospital · CNShanghai Advanced Research Institute · CN

Funding

National Natural Science Foundation of China (National Science Foundation of China) 32200016National Natural Science Foundation of China (National Science Foundation of China) 32222001National Natural Science Foundation of China (National Science Foundation of China) 32370028National Natural Science Foundation of China (National Science Foundation of China) U1967217Natural Science Foundation of Zhejiang Province (Zhejiang Provincial Natural Science Foundation) LDQ23C050002Natural Science Foundation of Zhejiang Province (Zhejiang Provincial Natural Science Foundation) LQ23C010002
6 · The paper itself

Abstract

Bacteria have evolved various response systems to adapt to environmental stress. A protease-based derepression mechanism in response to DNA damage was characterized in Deinococcus, which is controlled by the specific cleavage of repressor DdrO by metallopeptidase PprI (also called IrrE). Despite the efforts to document the biochemical, physiological, and downstream regulation of PprI-DdrO, the upstream regulatory signal activating this system remains unclear. Here, we show that single-stranded DNA physically interacts with PprI protease, which enhances the PprI-DdrO interactions as well as the DdrO cleavage in a length-dependent manner both in vivo and in vitro. Structures of PprI, in its apo and complexed forms with single-stranded DNA, reveal two DNA-binding interfaces shaping the cleavage site. Moreover, we show that the dynamic monomer-dimer equilibrium of PprI is also important for its cleavage activity. Our data provide evidence that single-stranded DNA could serve as the signal for DNA damage sensing in the metalloprotease/repressor system in bacteria. These results also shed light on the survival and acquired drug resistance of certain bacteria under antimicrobial stress through a SOS-independent pathway.

Indexed as

DeinococcusPeptide HydrolasesBacterial ProteinsDNA DamageDNA, Single-StrandedEndopeptidasesMetalloproteasesBacterial ProteinsDNA, Single-StrandedEndopeptidasesMetalloproteasesPeptide Hydrolases

Identifiers

PMID38424107
PMCPMC10904395
OpenAlexW4392282810

What OpenQuestion holds

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Registered trials

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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.