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Biochem Biophys Res Commun. 1990 Feb 14;166(3):1110-7.

Netropsin, distamycin and berenil interact differentially with a high-affinity binding site for the high mobility group protein HMG-I.

Author information

1
Institut für Biochemie, Universität Würzburg, Germany.

Abstract

Netropsin, distamycin, berenil and the chromosomal protein HMG-I share the ability to bind preferentially to AT-rich regions of DNA. We studied the binding behaviour of the chemical agents towards a high-affinity binding site for HMG-I by DNase I and MPE footprinting and analyzed their ability to challenge HMG-I-DNA complexes by competition experiments. Significant differences in the binding affinities and in the efficiencies to abolish HMG-I-DNA complexes were observed for the three drugs. Netropsin proved to be the most avidly binding compound and the most efficient competitor raising the interesting possibility that netropsin affects cell growth by interfering with HMG-I-DNA interaction.

PMID:
2154972
DOI:
10.1016/0006-291x(90)90981-r
[Indexed for MEDLINE]

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