חיפוש מתקדם
PLoS ONE
Oberpichler, I., Karlsruhe Institute of Technology (KIT), Botany I, Karlsruhe, Germany
Pierik, A.J., Philipps University, Institute of Cytobiology and Pathology, Core facility for Protein Spectroscopy, Marburg, Germany
Wesslowski, J., Karlsruhe Institute of Technology (KIT), Botany I, Karlsruhe, Germany
Pokorny, R., Philipps University, Plant Physiology and Photobiology, Marburg, Germany
Rosen, R., Agentek (1987) Ltd., Atidim Scientific Park, Tel Aviv, Israel
Vugman, M., Department of Molecular Microbiology and Biotechnology, The George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel
Zhang, F., Karlsruhe Institute of Technology (KIT), Botany I, Karlsruhe, Germany
Neubauer, O., Humboldt University Berlin, Institute for Microbiology, Berlin, Germany
Ron, E.Z., Department of Molecular Microbiology and Biotechnology, The George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel
Batschauer, A., Philipps University, Plant Physiology and Photobiology, Marburg, Germany
Lamparter, T., Karlsruhe Institute of Technology (KIT), Botany I, Karlsruhe, Germany
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. © 2011 Oberpichler et al.
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A photolyase-like protein from agrobacterium tumefaciens with an iron-sulfur cluster
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Oberpichler, I., Karlsruhe Institute of Technology (KIT), Botany I, Karlsruhe, Germany
Pierik, A.J., Philipps University, Institute of Cytobiology and Pathology, Core facility for Protein Spectroscopy, Marburg, Germany
Wesslowski, J., Karlsruhe Institute of Technology (KIT), Botany I, Karlsruhe, Germany
Pokorny, R., Philipps University, Plant Physiology and Photobiology, Marburg, Germany
Rosen, R., Agentek (1987) Ltd., Atidim Scientific Park, Tel Aviv, Israel
Vugman, M., Department of Molecular Microbiology and Biotechnology, The George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel
Zhang, F., Karlsruhe Institute of Technology (KIT), Botany I, Karlsruhe, Germany
Neubauer, O., Humboldt University Berlin, Institute for Microbiology, Berlin, Germany
Ron, E.Z., Department of Molecular Microbiology and Biotechnology, The George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel
Batschauer, A., Philipps University, Plant Physiology and Photobiology, Marburg, Germany
Lamparter, T., Karlsruhe Institute of Technology (KIT), Botany I, Karlsruhe, Germany
A photolyase-like protein from agrobacterium tumefaciens with an iron-sulfur cluster
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. © 2011 Oberpichler et al.
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