ArticleNucleic acids research2020
A topologically distinct class of photolyases specific for UV lesions within single-stranded DNA.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Role of photolyase in stress tolerance and virulence of plant-pathogenic bacteriumApplied and environmental microbiology · 2026Article
- Antarctic MicroalgaMarine drugs · 2026Article
- FeSBCP analogue from cyanobacteria: insights from in vitro and in silico studies.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2025Article
- UV damage induces production of mitochondrial DNA fragments with specific length profiles.Genetics · 2024Article
- UV damage induces production of mitochondrial DNA fragments with specific length profiles.bioRxiv : the preprint server for biology · 2023Article
- Article
- Multiple Profile Models Extract Features from Protein Sequence Data and Resolve Functional Diversity of Very Different Protein Families.Molecular biology and evolution · 2022Article
- Identification of a Novel Class of Photolyases as Possible Ancestors of Their Family.Molecular biology and evolution · 2021Article
- Ultrafast photoreduction dynamics of a new class of CPD photolyases.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2021Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Photolyases are ubiquitously occurring flavoproteins for catalyzing photo repair of UV-induced DNA damages. All photolyases described so far have a bilobal architecture with a C-terminal domain comprising flavin adenine dinucleotide (FAD) as catalytic cofactor and an N-terminal domain capable of harboring an additional antenna chromophore. Using sequence-similarity network analysis we discovered a novel subgroup of the photolyase/cryptochrome superfamily (PCSf), the NewPHLs. NewPHL occur in bacteria and have an inverted topology with an N-terminal catalytic domain and a C-terminal domain for sealing the FAD binding site from solvent access. By characterizing two NewPHL we show a photochemistry characteristic of other PCSf members as well as light-dependent repair of CPD lesions. Given their common specificity towards single-stranded DNA many bacterial species use NewPHL as a substitute for DASH-type photolyases. Given their simplified architecture and function we suggest that NewPHL are close to the evolutionary origin of the PCSf.
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