title: Netropsin, distamycin and berenil interact differentially with a high-affinity binding site for the high mobility group protein HMG-I.
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.
authors.affiliation: Institut für Biochemie, Universität Würzburg, Germany.
authors.forename: M
authors.initials: M
authors.lastname: Wegner
authors.forename: F
authors.initials: F
authors.lastname: Grummt
mesh_terms: D000578:Amidines / Q000378:metabolism*; D000981:Antiprotozoal Agents / Q000378:metabolism*; D001483:Base Sequence; D001665:Binding Sites; D004247:DNA / Q000187:drug effects / Q000378:metabolism*; D003850:Deoxyribonuclease I; D004133:Diminazene / Q000031:analogs & derivatives / Q000378:metabolism* / Q000494:pharmacology; D004214:Distamycins / Q000378:metabolism* / Q000494:pharmacology; D006146:Guanidines / Q000378:metabolism*; D006609:High Mobility Group Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D009429:Netropsin / Q000378:metabolism* / Q000494:pharmacology; D010957:Plasmids; D011758:Pyrroles / Q000378:metabolism*
chemical_list: D000578:Amidines; D000981:Antiprotozoal Agents; D004214:Distamycins; D006146:Guanidines; D006609:High Mobility Group Proteins; D011758:Pyrroles; D009429:Netropsin; D004247:DNA; D003850:Deoxyribonuclease I; C003915:diminazene aceturate; D004133:Diminazene