Proton NMR study on a histone-like protein HU(α), from Escherichia coli and its complex with oligo DNAs

H. Shindo*, H. Kurumizaka, A. Furubayashi, C. Sakuma, U. Matsumoto, A. Yanagida, N. Goshima, Y. Kano, F. Imamoto

*この研究の対応する著者

研究成果: Article査読

6 被引用数 (Scopus)

抄録

It was confirmed that the flexible arm region of HU(α) forms an antiparallel β-sheet and that all of the residues of phenylalanines, together with some of leucines and/or valines, form a hydrophobic core within the dimer of HU(α). HU(α) protein alone is thermally labile and melts at 38 °C, but it becomes remarkably stabilized and melts at 59 °C in the presence of DNA. Several resonances from both HL(α) and DNA perturbed by their complex formation, notably those of His C-2 and C-4 protons, downfield shifted C(α) protons in the antiparallel β-sheet, as well as Arg C(δ) and Lys C(ε) protons. The results indicated that a β-sheet region of HU(α) binds to DNA, and also showed that rapid equilibrium occurs on the NMR time scale between bound and unbound states of HU(α). A few intermolecular nuclear Overhauser effects (NOEs) were also observed between the protein and H1' protons of DNA in the complex, suggesting that HU(α) binds primarily to the minor groove of DNA.

本文言語English
ページ(範囲)437-443
ページ数7
ジャーナルBiological and Pharmaceutical Bulletin
16
5
出版ステータスPublished - 1993
外部発表はい

ASJC Scopus subject areas

  • 分子医療
  • 薬理学、毒性学および薬学(全般)

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