Proton NMR Study on a Histone-like Protein, HU_α, from Escherichia coli and Its Complex with Oligo DNAs

概要

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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℃, but it becomes remarkably stabilized and melts at 59℃ in the presence of DNA. Several resonances from both HU_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.
公益社団法人日本薬学会の論文
1993-05-15