Evidence map›Paper›PMID 40890820›Full record

ArticleJournal of biological engineering2025

Efficient site-specific recombination by self-activating split-Dre recombinase in mammalian cells and E. coli.

Chichu Xie, Jinfeng Gan, Yuanhao Zhang, Wentao Yu, Ruirui Li, Dan Yu, Yu Liu, Song Guo Zheng, Guangying Qi

Abstract read
In one paragraph

Article in Journal of biological engineering, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

9 authors.

Chichu Xie *Guangxi Key Laboratory of Tumor Immunology and Microenvironmental Regulation, Guilin Medical University, Guilin, 541199, China. xcc335@glmu.edu.cn.
Jinfeng Gan *Guangxi Key Laboratory of Tumor Immunology and Microenvironmental Regulation, Guilin Medical University, Guilin, 541199, China.
Yuanhao ZhangGuangxi Key Laboratory of Tumor Immunology and Microenvironmental Regulation, Guilin Medical University, Guilin, 541199, China.
Wentao YuGuangxi Key Laboratory of Tumor Immunology and Microenvironmental Regulation, Guilin Medical University, Guilin, 541199, China.
Ruirui LiGuangxi Key Laboratory of Tumor Immunology and Microenvironmental Regulation, Guilin Medical University, Guilin, 541199, China.
Dan YuGuangxi Key Laboratory of Tumor Immunology and Microenvironmental Regulation, Guilin Medical University, Guilin, 541199, China.
Yu LiuGuangxi Key Laboratory of Tumor Immunology and Microenvironmental Regulation, Guilin Medical University, Guilin, 541199, China.
Song Guo ZhengDepartment of Rheumatology & Immunology, School of Cell and Gene Therapy, Songjiang Research Institute, Songjiang Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 201600, China. Zheng@osumc.edu.
Guangying QiGuangxi Key Laboratory of Tumor Immunology and Microenvironmental Regulation, Guilin Medical University, Guilin, 541199, China. qgy@glmu.edu.cn.

Funding

Guangxi Science and Technology Program GuiKeAD23026143
6 · The paper itself

Abstract

backgroundSite-specific recombination (SSR) systems are essential tools for conditional genetic manipulation and are valued for their efficacy and user friendliness. However, the development of novel SSR strategies is urgently needed. This study aimed to identify a split Dre protein configuration that can self-activate.

resultsBy exploiting the homology between Dre and Cre, we designed a strategy to split the Dre protein at specific amino acid residues and systematically pair the resulting peptide fragments. Among these combinations, the N191/192C pair exhibited detectable recombinase activity when mediating recombination between episomal rox sites in 293T cells, whereas the other pairs presented minimal recombinase activity. Subsequent experiments revealed that the N191/192C combination efficiently mediated site-specific recombination at the integrated rox sites, without the need for auxiliary protein fusions, and demonstrated recombinase activity that is at least equivalent to that of the intact Dre protein. Interestingly, while fusion with the intein peptide increased the activity of N60/61C pair, it had a deleterious effect on the N191/192C pair. The N191/192C combination also displayed robust recombinase activity in both the murine 4T1 cell line and E. coli bacteria. Finally, our experiments demonstrated that there was no detectable cross-complementation between the split Dre and split Cre proteins.

conclusionsThe N191/192C split Dre protein and the intein-fused N60/61C split Dre protein can effectively mediate recombination of the integrated rox sites without the need for external signals such as light or chemical compounds. Split Dre and Cre proteins can be used together in the same cell without interfering with each other. These findings introduce new tools and strategies for gene editing and the generation of transgenic animals.

Indexed as

DreProtein fragment complementationSite-specific recombination

Identifiers

PMID40890820
PMCPMC12403448

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.