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Purification and characterization of a novel DNA repair enzyme from the extremely radioresistant bacterium Rubrobacter radiotolerans

Asgarani, E ; Terato, H ; Asagoshi, K ; Shahmohammadi, H R ; Ohyama, Y ; Saito, T ; Yamamoto, O ; Ide, H

Journal of radiation research, 2000, Vol.41 (1), p.19-34 [Periódico revisado por pares]

England: Oxford University Press

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Título:
Purification and characterization of a novel DNA repair enzyme from the extremely radioresistant bacterium Rubrobacter radiotolerans
Autor: Asgarani, E ; Terato, H ; Asagoshi, K ; Shahmohammadi, H R ; Ohyama, Y ; Saito, T ; Yamamoto, O ; Ide, H
Assuntos: Apurinic Acid - analysis ; Arthrobacter - enzymology ; Arthrobacter - genetics ; Arthrobacter - radiation effects ; Bacterial Proteins - genetics ; Bacterial Proteins - isolation & purification ; Deoxyribonuclease (Pyrimidine Dimer) ; DNA Damage ; DNA Ligases - genetics ; DNA Ligases - isolation & purification ; DNA Repair - genetics ; DNA, Bacterial - genetics ; DNA, Bacterial - radiation effects ; Electrophoresis, Polyacrylamide Gel ; Endodeoxyribonucleases - metabolism ; Endonucleases - chemistry ; Endonucleases - genetics ; Endonucleases - isolation & purification ; Escherichia coli ; Escherichia coli Proteins ; Radiation Tolerance - genetics ; Radon ; Rubrobacter radiotolerans ; Substrate Specificity ; Thymine - analogs & derivatives ; Thymine - metabolism ; Urea - metabolism ; Water Microbiology
É parte de: Journal of radiation research, 2000, Vol.41 (1), p.19-34
Notas: ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
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Descrição: Rubrobacter radiotolerans is an extremely radioresistant bacterium. It exhibits higher resistance than the well-known radioresistant bacterium Deinococcus radiodurans, but the molecular mechanisms responsible for the radio-resistance of R. radiotolerans remain unknown. In the present study, we have demonstrated the presence of a novel DNA repair enzyme in R. radiotolerans cells that recognizes radiation-induced DNA damages such as thymine glycol, urea residues, and abasic sites. The enzyme was purified from the crude cell extract by a series of chromatography to an apparent physical homogeneity. The purified enzyme showed a single band with a molecular mass of approximately 40 kDa in SDS-polyacrylamide gel electrophoresis, and was designated as R-endonuclease. R-Endonuclease exhibited repair activity for thymine glycol, urea residues, and abasic sites present in plasmid DNA, but did not act on intact DNA, UV-irradiated DNA and DNA containing reduced abasic sites. The substrate specificity together with the salt and pH optima suggests that R-endonuclease is a functional homolog of endonuclease III of Escherichia coli.
Editor: England: Oxford University Press
Idioma: Inglês

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Purification and characterization of a novel DNA repair enzyme from the extremely radioresistant bacterium Rubrobacter radiotolerans

Asgarani, E ; Terato, H ; Asagoshi, K ; Shahmohammadi, H R ; Ohyama, Y ; Saito, T ; Yamamoto, O ; Ide, H

England: Oxford University Press

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