Plant PAXX has an XLF-like function and stimulates DNA end-joining by the Ku-DNA ligase IV-XRCC4 complex
Open accessPreprint — published as 10.1111/tpj.16359 · Paper page
Abstract
Non-homologous end joining (NHEJ) plays a major role in repairing DNA double-strand breaks (DSBs) and is key to genome stability and editing. The minimal core NHEJ proteins, namely Ku70, Ku80, DNA ligase IV and XRCC4, are conserved, but other factors vary in different eukaryotes groups. In plants, known NHEJ proteins are the core factors only, and the molecular mechanism of plant NHEJ remains unclear. Here, we report a previously unidentified plant ortholog of PAXX, the crystal structure of which showed a similar fold to human PAXX. However, plant PAXX has similar molecular functions to human XLF, by directly interacting with Ku70/80 and XRCC4. This suggests that plant PAXX combines the roles of mammalian PAXX and XLF and that these functions merged into a single protein during evolution. This is consistent with a redundant function of PAXX and XLF in mammals.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
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- Authors
- Khan, H., & Ochi, T.
- Affiliations
- University of Leeds (GB)
- Corresponding author
- Ochi, Takashi
- ORCID
- Ochi, Takashi
- Venue
- The Plant Journal
- Publisher
- openRxiv
- Published
- 2023-05-28
- Volume
- 116
- Issue
- 1
- Pages
- 58-68
- ISSN
- 0960-7412 (ISSN-L)
- OpenAlex
- W4381470271
- Cited by
- 8
- References
- 1
- Citations by year
- 2025: 3 · 2024: 2 · 2023: 3
- FWCI
- 0.71
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc
- Locations
- The Plant Journal (publishedVersion, cc-by-nc)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc)
- PubMed (publishedVersion)
- White Rose Research Online (University of Leeds, The University of Sheffield, University of York) (acceptedVersion, cc-by-nc)
- Funders
- University of Leeds
- Biotechnology and Biological Sciences Research Council (BB/V003577/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › CRISPR and Genetic Engineering
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Keywords
- PAXX, X-ray luminosity function, non-homologous end joining, DNA double-strand break repair, Ku70/80, DNA ligase IV, XRCC4, DNA end joining, plant DNA repair, protein crystal structure, protein evolution, genome stability
- MeSH terms
- DNA Ligase ATP, Animals, DNA, DNA-Binding Proteins, Humans, Mammals, Trisaccharides, DNA Repair Enzymes, DNA End-Joining Repair
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