Proteins from the prokaryotic nucleoid. Interaction of nucleic acids with the 15 kDa Escherichia coli histone-like protein H-NS

FEBS Letters
K FriedrichC L Pon

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 x SSC binds DNA with an apparent Ka approximately equal to 1.1 x 10(4) 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.

References

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Aug 9, 2001·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·T Ohyama
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Related Concepts

poly(dC-dG)
HU-2 protein, Bacteria
Bacterial Proteins
Chromatography, Affinity
DNA Helix Destabilizing Proteins
DNA, Bacterial
DNA, Single-Stranded
d(A(5)T(5))2
Polydeoxyribonucleotides
RNA, Bacterial

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