Characterization of a thermostable DNA photolyase from an extremely thermophilic bacterium, Thermus thermophilus HB27

  • Kato R
  • Hasegawa K
  • Hidaka Y
 et al. 
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Abstract

he photolyase gene from Thermus thermophilus was cloned and sequenced. The characteristic absorption and fluorescence spectra of the purified T. thermophilus photolyase suggested that the protein has FAD as a chromophore. The second chromophore binding site was not conserved in T. thermophilus photolyase. The purified enzyme showed light-dependent photoreactivation activity in vitro at 35 and 65° and was stable when subjected to heat and acidic pH.

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Authors

  • Ryuichi Kato

  • Koichi Hasegawa

  • Yuki Hidaka

  • Seiki Kuramitsu

  • Takayuki Hoshino

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