title: Divalent Cations Increase DNA Repair Activities of Bacterial (6-4) Photolyases.
abstract: The (6-4) photolyases of the FeS-BCP group can be considered as the most ancient type among the large family of cryptochrome and photolyase flavoproteins. In contrast to other photolyases, they contain an Fe-S cluster of unknown function, a DMRL chromophore, an interdomain loop, which could interact with DNA, and a long C-terminal extension. We compared DNA repair and photoreduction of two members of the FeS-BCP family, Agrobacterium fabrum PhrB and Rhodobacter sphaeroides RsCryB, with a eukaryotic (6-4) photolyase from Ostreococcus, OsCPF, and a member of the class III CPD photolyases, PhrA from A. fabrum. We found that the low DNA repair effectivity of FeS-BCP proteins is largely stimulated by Mg2+and other divalent cations, whereas no effect of divalent cations was observed in OsCPF and PhrA. The (6-4) repair activity in the presence of Mg2+is comparable with the repair activities of the other two photolyases. The photoreduction, on the other hand, is negatively affected by Mg2+in PhrB, but stimulated by Mg2+in PhrA. A clear relationship of Mg2+dependency on DNA repair with the evolutionary position conflicts with Mg2+dependency of photoreduction. We discuss the Mg2+effect in the context of structural data and DNA binding.
authors.affiliation: Karlsruhe Institute of Technology, Botanical Institute, Karlsruhe, Germany.
authors.forename: Hongju
authors.initials: H
authors.lastname: Ma
authors.affiliation: China Academy of Engineering Physics, Institute of Materials, Mianyang, China.
authors.forename: Fan
authors.initials: F
authors.lastname: Zhang
authors.affiliation: Department of Chemistry, LOEWE Center for Synthetic Microbiology, Philipps University Marburg, Marburg, Germany.
authors.forename: Elisabeth
authors.initials: E
authors.lastname: Ignatz
authors.affiliation: Karlsruhe Institute of Technology, Botanical Institute, Karlsruhe, Germany.
authors.forename: Martin
authors.initials: M
authors.lastname: Suehnel
authors.affiliation: Karlsruhe Institute of Technology, Botanical Institute, Karlsruhe, Germany.
authors.forename: Peng
authors.initials: P
authors.lastname: Xue
authors.affiliation: Institute of Medical Physics and Biophysics (CC2), Group Protein X-ray Crystallography and Signal Transduction, Charité - Universitätsmedizin Berlin, Berlin, Germany.
authors.forename: Patrick
authors.initials: P
authors.lastname: Scheerer
authors.affiliation: Department of Chemistry, LOEWE Center for Synthetic Microbiology, Philipps University Marburg, Marburg, Germany.
authors.forename: Lars Oliver
authors.initials: LO
authors.lastname: Essen
authors.affiliation: Karlsruhe Institute of Technology, Botanical Institute, Karlsruhe, Germany.
authors.forename: Norbert
authors.initials: N
authors.lastname: Krauß
authors.affiliation: Karlsruhe Institute of Technology, Botanical Institute, Karlsruhe, Germany.
authors.forename: Tilman
authors.initials: T
authors.lastname: Lamparter
mesh_terms: D060054:Agrobacterium / Q000201:enzymology* / Q000235:genetics; D020134:Catalytic Domain; D002413:Cations, Divalent; D000460:Chlorophyta / Q000201:enzymology*; D004260:DNA Repair; D004269:DNA, Bacterial / Q000378:metabolism; D018744:DNA, Plant / Q000378:metabolism; D004255:Deoxyribodipyrimidine Photo-Lyase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007506:Iron-Sulfur Proteins / Q000378:metabolism; D008027:Light; D008274:Magnesium / Q000378:metabolism*; D016296:Mutagenesis; D010084:Oxidation-Reduction; D012242:Rhodobacter sphaeroides / Q000201:enzymology*
chemical_list: D002413:Cations, Divalent; D004269:DNA, Bacterial; D018744:DNA, Plant; D007506:Iron-Sulfur Proteins; C098727:pyrimidine(6-4)pyrimidone photolyase; D004255:Deoxyribodipyrimidine Photo-Lyase; D008274:Magnesium