Carboxyl terminal region of the MukB protein in Escherichia coli is essential for DNA binding activity

Authors

  • Abu Z.M. Saleh,

    1. Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University School of Medicine, Kuhonji 4-24-1, Kumamoto 862, Japan
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  • Kunitoshi Yamanaka,

    1. Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University School of Medicine, Kuhonji 4-24-1, Kumamoto 862, Japan
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  • Hironori Niki,

    1. Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University School of Medicine, Kuhonji 4-24-1, Kumamoto 862, Japan
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  • Teru Ogura,

    1. Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University School of Medicine, Kuhonji 4-24-1, Kumamoto 862, Japan
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  • Mitsuyoshi Yamazoe,

    1. Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University School of Medicine, Kuhonji 4-24-1, Kumamoto 862, Japan
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  • Sola Hiraga

    Corresponding author
    1. Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University School of Medicine, Kuhonji 4-24-1, Kumamoto 862, Japan
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*Corresponding author. Tel.: +81 (96) 373-5334; Fax: +81 (96) 371-2408; E-mail: hiraga@gpo.kumamoto-u.ac.jp

Abstract

Abstract The purified MukB protein of Escherichia coli has DNA binding activity and nucleotide binding activity. We have isolated a mutation, mukB1013, causing a substitution of valine at position 1379 to leucine. This mutant MukB protein was defective for DNA binding, while the ATP binding activity remained unaffected. A truncated MukB protein that is short of 109 amino acids from the C-terminus failed to bind DNA.

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