Aspects of specific DNA-protein interaction; local bending of DNA molecules by in-register binding of the oligopeptide antibiotic distamycin

Reinert, K.E.

doi:10.1016/0301-4622(81)80019-1

Cited by 38 publications

(10 citation statements)

References 46 publications

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“…Therefore our viscosity data on the individual modes on SN-6999 binding to three different DNA samples can be intetpreted as a preferential binding of this drug to dA · dT clusters in DNA Our data clearly demonstrate that both Nt and SN-6999 exhibit very similar dA · dT-cluster specificity which might originate from very similar energetical and conformational aspects in their binding to DNA The respective similarities may partially reside in corresponding functional H-donors ofNH groups and their favourable positioning in the ligand structure as discussed below. In contrast to these two ligands, Dst-3 exhibits a very different DNA response characterized by DNA helix bending, which obviously originates Downloaded by [Rutgers University] at 13:54 12 April 2015 from the lacking of the guanidino group on one end of the oligopeptide (26).…”

Section: Viscosimetric Studiesmentioning

confidence: 97%

Interaction of the Nonintercalative Antitumour Drugs SN-6999 and SN-18071 with DNA: Influence of Ligand Structure on the Binding Specificity

Luck¹,

Reinert²,

Baguley

et al. 1987

Journal of Biomolecular Structure and Dynamics

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Binding to DNA's of the non-intercalative ligands SN-6999 and SN-18071 has been studied by means of circular dichroism, UV absorption, thermal melting and for SN-6999 by viscosity measurements. Both antitumour drugs show a preference for dA.dT rich DNA's, but the base pair selectivity of SN-18071 is lower as indicated by some affinity to dG.dC containing duplex DNA. The dA.dT base pair specificity of SN-6999 is comparable to that of netropsin. It forms very stable complexes with dA.dT containing duplex DNA and competes with netropsin binding on DNA. The ligands SN-18071 and pentamidine are totally released from their complexes with poly(dA-dT).poly(dA-dT) by competitive netropsin binding. The results demonstrate that hydrogen bonding capacity of the ligand in addition to other factors strongly contribute to the base sequence specificity in the recognition process of the ligand with DNA. A binding model of SN-6999 with five dA.dT pairs in the minor groove of B-DNA is suggested.

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Section: Viscosimetric Studiesmentioning

confidence: 97%

Interaction of the Nonintercalative Antitumour Drugs SN-6999 and SN-18071 with DNA: Influence of Ligand Structure on the Binding Specificity

Luck¹,

Reinert²,

Baguley

et al. 1987

Journal of Biomolecular Structure and Dynamics

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“…The explanation may lie in the known deviations in DNA-binding effects between netropsin and distamycin A. The pronounced effect of distamycin A may also be understood on the basis of previously reported viscosity changes in hydrody namic studies (Reinert, 1981), from which it was concluded that netropsin causes stiffening and elongation of the bound DNA regions (Reinert, 1972), whereas distamycin A, showing a lower ing in viscosity within the low concentration range of the ligand, may produce local bending of the DNA molecule (Reinert, 1981).…”

Section: Dna Binding Ofdapi Distamycin a And Related Ligandsmentioning

confidence: 92%

“…whereas distamycin A is bound to the DNA helix in a crystalline structure with a stable, propeller-twist con formation. These differences in binding conformation between netropsin and distamycin A, especially the bending of distamy cin A-bound DNA segments (Reinert, 1981), may bestow on distamycin A its greater capacity to exclude DAPI from its bind ing sites.…”

Section: Dna Binding Ofdapi Distamycin a And Related Ligandsmentioning

confidence: 99%

Mechanisms of distamycin A/DAPI chromosome staining

Burckhardt

Votavová

Jantsch

et al. 1993

Cytogenet Genome Res

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The molecular mechanism underlying distamycin A-induced differential DAPI fluorescent staining of metaphase chromosomes was studied in Sus scrofa domestica both cytologically, using, besides DAPI, two isomeric derivatives of DAPI (D288.45 and D288.48), and molecularly, by in vitro competitive-binding studies using 5”. scrofa satellite DNA and synthetic DNA polymers. Significant differences in heterochromatin staining were observed between D288.45 and D288.48. Distinct distamycin A/DAPI bands were obtained with DAPI and D288.45 but not with D288.48. Circular dichroism measurements were performed to characterize the displacement of DAPI from its DNA binding sites by distamycin A and also netropsin. Distamycin A was most effective in displacing DAPI when DAPI was bound to contiguous clusters of AT base pairs and much less effective in displacing DAPI bound to GC or mixed AT/GC base-pair sequences. The results of these competitive-binding studies provide the basis of a molecular explanation of the quenching phenomenon of distamycin A counterstaining on chromosomal DAPI fluorescence.

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“…For non-cooperative DNA-ligand interaction and small a values, the 1/a(r) curves are almost symmetrical ( 4). Individual peculiarities are pointed out by the quantitative treatment.…”

Section: Introductionmentioning

confidence: 96%

“…Details are given in the accompanying paper (2). For bending angles y~So, the change of persistence length is fairly sensitive to ligand-induced helix bending (4).…”

Section: Introductionmentioning

confidence: 99%

DNA-Bending on Ligand Binding; Change of DNA Persistence Length

Schü¹,

Reinert²

1991

Journal of Biomolecular Structure and Dynamics

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This paper simulates the helix-characteristic changes of apparent DNA persistence length caused by randomly distributed helix bends as induced, e.g., by DNA-bound ligand molecules. The parameters varied are the constant angle gamma of helix bending and the size alpha of the DNA drug binding site, but also the degree of DNA-ligand binding cooperativity and the helix-unwinding angle. If the size of the binding site is comparable with the helix pitch, the influence of phasing between helix bends and helix screw upon the apparent persistence length is obvious. In the accompanying paper experimental data are analyzed in terms of this theoretical background.

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Aspects of specific DNA-protein interaction; local bending of DNA molecules by in-register binding of the oligopeptide antibiotic distamycin

Cited by 38 publications

References 46 publications

Interaction of the Nonintercalative Antitumour Drugs SN-6999 and SN-18071 with DNA: Influence of Ligand Structure on the Binding Specificity

Interaction of the Nonintercalative Antitumour Drugs SN-6999 and SN-18071 with DNA: Influence of Ligand Structure on the Binding Specificity

Mechanisms of distamycin A/DAPI chromosome staining

DNA-Bending on Ligand Binding; Change of DNA Persistence Length

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