Arginine-55 in the β-arm is essential for the activity of DNA-binding protein HU from bacillu

Fumiyo Saitoh, Shunsuke Kawamura, Nobuyuki Yamasaki, Isao Tanaka, Makoto Kimura

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Abstract

DNA-binding protein HU (BstHU) from Bacillus stearothermophilus is a homodimeric protein which binds to DNA in a sequence-nonspecific manner. In order to identify the Arg residues essential for DNA binding, four Arg residues (Arg-53, Arg-55, Arg-58, and Arg-61) within the β-arm structure were replaced either by Gln, Lys, or Glu residues, and the resulting mutants were characterized with respect to their DNA-binding activity by a filter-binding analysis and surface plasmon resonance analysis. The results indicate that three Arg residues (Arg-55, Arg-58, and Arg-61) play a crucial role in DNA binding as positively charged recognition groups in the order of Arg-55>Arg-58>Arg-61 and that these are required to decrease the dissociation rate constant for BstHU-DNA interaction. In contrast, the Arg-53 residue was found to make no contribution to the binding activity of BstHU.

Original languageEnglish
Pages (from-to)2232-2235
Number of pages4
JournalBioscience, Biotechnology and Biochemistry
Volume63
Issue number12
DOIs
Publication statusPublished - Jan 1 1999

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All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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