Evidence map›Paper›PMID 40689749›Full record

ArticleProtein science : a publication of the Protein Society2025

Bacterial PprI-DdrO system evolved from ImmA-ImmR system in the prophage.

Linjia Wang, Shitong Zhong, Shuang Song, Liangyan Wang, Yuejin Hua, Huizhi Lu

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Bacterial PprI-DdrO system evolved from ImmA-ImmR system in the prophage.Protein science : a publication of the Protein Society · 2025
    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

6 authors.

Linjia WangMOE 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.
Shuang SongMOE Key Laboratory of Biosystems Homeostasis & Protection, Institute of Biophysics, College of Life Sciences, Zhejiang University, Hangzhou, China.
Liangyan WangMOE Key Laboratory of Biosystems Homeostasis & Protection, Institute of Biophysics, College of Life Sciences, Zhejiang University, Hangzhou, China.
Yuejin HuaMOE Key Laboratory of Biosystems Homeostasis & Protection, Institute of Biophysics, College of Life Sciences, Zhejiang University, Hangzhou, China.ORCID 0000-0001-6743-0919
Huizhi LuMOE Key Laboratory of Biosystems Homeostasis & Protection, Institute of Biophysics, College of Life Sciences, Zhejiang University, Hangzhou, China.ORCID 0000-0002-2408-4427

Funding

National Natural Science Foundation of China 32200016National Natural Science Foundation of China 32370028Zhejiang Provincial Natural Science Foundation of China LGN22C010002Zhejiang Provincial Natural Science Foundation of China LQ23C010002Zhejiang Provincial Natural Science Foundation of China LZYQ25C010002
6 · The paper itself

Abstract

Organisms have evolved various response systems to cope with DNA damage, such as the PprI-DdrO system and the ImmA-ImmR system, which mediate the transcription of DNA damage response genes or facilitate the transfer of DNA elements upon sensing DNA damage. The two systems are functionally analogous, and their metalloproteases and regulators are each classified into the same respective protein families, indicating an evolutionary relationship between them. In this article, we analyzed the homology and evolutionary relationship between the ImmA-ImmR and PprI-DdrO. Significant similarities among these proteins were observed through sequence and structure alignments, and the functional association of these protein pairs was confirmed by in silico and biochemical experiments. Furthermore, we revealed a series of protein pairs resembling PprI-DdrO across various species, including ImmA-ImmR from Deinococcus phage elements. Through phylogenetic analysis, we found that these ImmA-ImmR systems share the same major clade with PprI-DdrO. These results revealed a significant association between the PprI-DdrO and ImmA-ImmR systems, inferring that the PprI-DdrO system originated from the ImmA-ImmR system within prophage elements.

Indexed as

Bacterial ProteinsEvolution, MolecularProphagesViral ProteinsDNA DamagePhylogenyBacterial ProteinsViral ProteinsDeinococcusevolutionImmA–ImmRPprI–DdrO

Identifiers

PMID40689749
PMCPMC12278698

What OpenQuestion holds

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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.