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• W1998897210 abstract "The interaction between nucleic acids and Escherichia coli H-NS, an abundant 15 kDa histone-like protein, has been studied by affinity chromatography, nitrocellulose filtration and fluorescence spectroscopy. Intrinsic fluorescence studies showed that the single Trp residue of H-NS (position 108) has a restricted mobility and is located within an hydrophobic region inaccessible to both anionic and cationic quenchers. Binding of H-NS to nucleic acids, however, results in a change of the microenvironment of the Trp residue and fluorescence quenching; from the titration curves obtained with addition of increasing amounts of poly(dA)-poly(dT) and poly(dC)-poly(dG) it can be estimated that an H-NS dimer in 1.5 × SSC binds DNA with an apparent K a−1.1 × 104 M−1· bp−1. H-NS binds to double-stranded DNA with a higher affinity than the more abundant histone-like protein NS(HU) and, unlike NS, prefers double-stranded to single-stranded DNA and DNA to RNA; both monovalent and divalent cations are required for optimal binding." @default.
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• W1998897210 date "1988-02-29" @default.
• W1998897210 modified "2023-09-25" @default.
• W1998897210 title "Proteins from the prokaryotic nucleoid Interaction of nucleic acids with the 15 kDa<i>Escherichia coli</i>histone-like protein H-NS" @default.
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• W1998897210 doi "https://doi.org/10.1016/0014-5793(88)80826-3" @default.
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