Contribution of a salt bridge to the thermostability of DNA binding protein HU from Bacillus stearothermophilus determined by site-directed mutagenesis.

@article{Kawamura1997ContributionOA,
  title={Contribution of a salt bridge to the thermostability of DNA binding protein HU from Bacillus stearothermophilus determined by site-directed mutagenesis.},
  author={S. Kawamura and I. Tanaka and Nobuyuki Yamasaki and M. Kimura},
  journal={Journal of biochemistry},
  year={1997},
  volume={121 3},
  pages={
          448-55
        }
}
  • S. Kawamura, I. Tanaka, +1 author M. Kimura
  • Published 1997
  • Biology, Medicine
  • Journal of biochemistry
  • We have employed site-directed mutagenesis to evaluate the contribution of the amino acid residues, Glu34, Arg37, and Lys38, to the thermostability of the thermophilic protein, Bacillus stearothermophilus DNA binding protein HU (BstHU), relative to the mesophilic homologue, Bacillus subtilis HU (BsuHU). Mutants BstHU-E34D and BstHU-K38N, in which Glu34 and Lys38 were individually replaced by the corresponding residues, Asp34 and Asn38, in BsuHU, exhibited decreased thermostabilities by 2.08 and… CONTINUE READING
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