ArticlePloS one2011
A photolyase-like protein from Agrobacterium tumefaciens with an iron-sulfur cluster.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Role of photolyase in stress tolerance and virulence of plant-pathogenic bacteriumApplied and environmental microbiology · 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
- The Genetic Determinants of Extreme UV Radiation and Desiccation Tolerance in a Bacterium Recovered from the Stratosphere.Microorganisms · 2025Article
- Article
- Deconvolution of dynamic heterogeneity in protein structure.Structural dynamics (Melville, N.Y.) · 2024Review
- Dynamic interplays between three redox cofactors in a DNA photolyase revealed by spectral decomposition.Cell reports. Physical science · 2023Article
- The crystal structure of Vibrio cholerae (6-4) photolyase reveals interactions with cofactors and a DNA-binding region.The Journal of biological chemistry · 2023Article
- Article
- Identification and characterization of a prokaryotic 6-4 photolyase from Synechococcus elongatus with a deazariboflavin antenna chromophore.Nucleic acids research · 2022Article
- Identification of a Novel Class of Photolyases as Possible Ancestors of Their Family.Molecular biology and evolution · 2021Article
- Review
- Non-classical disproportionation revealed by photo-chemically induced dynamic nuclear polarization NMR.Magnetic resonance (Gottingen, Germany) · 2021Article
- A topologically distinct class of photolyases specific for UV lesions within single-stranded DNA.Nucleic acids research · 2020Article
- Review
- A (6-4)-photolyase from the Antarctic bacterium Sphingomonas sp. UV9: recombinant production and in silico features.Extremophiles : life under extreme conditions · 2020Article
- UvrC Coordinates an OJournal of the American Chemical Society · 2020Article
- Light Modulates the Physiology of NonphototrophicJournal of bacteriology · 2019Article
- Functional role of an unusual tyrosine residue in the electron transfer chain of a prokaryotic (6-4) photolyase.Chemical science · 2018Article
- Searching for novel photolyases in UVC-resistant Antarctic bacteria.Extremophiles : life under extreme conditions · 2017Article
- CRISPR System Acquisition and Evolution of an Obligate Intracellular Chlamydia-Related Bacterium.Genome biology and evolution · 2016Article
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Authors and funding
11 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Photolyases and cryptochromes are evolutionarily related flavoproteins with distinct functions. While photolyases can repair UV-induced DNA lesions in a light-dependent manner, cryptochromes regulate growth, development and the circadian clock in plants and animals. Here we report about two photolyase-related proteins, named PhrA and PhrB, found in the phytopathogen Agrobacterium tumefaciens. PhrA belongs to the class III cyclobutane pyrimidine dimer (CPD) photolyases, the sister class of plant cryptochromes, while PhrB belongs to a new class represented in at least 350 bacterial organisms. Both proteins contain flavin adenine dinucleotide (FAD) as a primary catalytic cofactor, which is photoreduceable by blue light. Spectral analysis of PhrA confirmed the presence of 5,10-methenyltetrahydrofolate (MTHF) as antenna cofactor. PhrB comprises also an additional chromophore, absorbing in the short wavelength region but its spectrum is distinct from known antenna cofactors in other photolyases. Homology modeling suggests that PhrB contains an Fe-S cluster as cofactor which was confirmed by elemental analysis and EPR spectroscopy. According to protein sequence alignments the classical tryptophan photoreduction pathway is present in PhrA but absent in PhrB. Although PhrB is clearly distinguished from other photolyases including PhrA it is, like PhrA, required for in vivo photoreactivation. Moreover, PhrA can repair UV-induced DNA lesions in vitro. Thus, A. tumefaciens contains two photolyase homologs of which PhrB represents the first member of the cryptochrome/photolyase family (CPF) that contains an iron-sulfur cluster.
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