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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)437-443
Number of pages7
JournalBiological and Pharmaceutical Bulletin
Issue number5
Publication statusPublished - 1993
Externally publishedYes


  • HU protein
  • HU-DNA complex
  • HU-DNA interaction
  • proton NMR
  • thermal stability

ASJC Scopus subject areas

  • Molecular Medicine
  • Pharmacology, Toxicology and Pharmaceutics(all)


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