Interaction of the oligopeptide antibiotics netropsin and distamycin a with nucleic acids

Zimmer, Ch.; Reinert, K.E.; Luck, G.; Wähnert, U.; Löber, G.; Thrum, H.

doi:10.1016/0022-2836(71)90250-6

Cited by 170 publications

(64 citation statements)

References 36 publications

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“…However, the presence of DA/DAPI negative bands may agree with the base-pair composition of this heterochromatic domain because distamycin has high affinity with and is specific to AT-rich domains, forming a very stable complex with DNA and causing structural changes in the double strand (Zimmer et al, 1971) which may reduce or block the accessibility of DAPI to the chromosomal DNA, as has been previously described for another A. scabripinnis population (Souza et al, 1996).…”

Section: Discussionsupporting

confidence: 64%

Evidence of the differentiated structural arrangement of constitutive heterochromatin between two populations of Astyanax scabripinnis (Pisces, Characidae)

et al. 2004

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The composition of heterochromatin classes along the chromosomes of specimens from two populations of the fish Astyanax scabripinnis was examined using fluorescence banding with GC-and AT-DNA specific fluorochromes and fluorescence in situ hybridization (FISH) with an AT-rich satellite DNA (As51) probe. For the pericentromeric heterochromatin blocks neither GC/AT-DNA specific fluorochromes nor the FISH technique produce any response with chromosomes from either of the populations. On the other hand, the telomeric distal heterochromatin blocks of both populations fluoresced when the FISH technique was applied but showed distinct responses after GC-specific fluorochrome treatments, leading us to propose different structural arrangements of the FISH-positive heterochromatins. Such differences in chromosome banding patterns together with other karyotypic differences suggest differentiation of these populations at taxonomic level.

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Section: Discussionsupporting

confidence: 64%

Evidence of the differentiated structural arrangement of constitutive heterochromatin between two populations of Astyanax scabripinnis (Pisces, Characidae)

et al. 2004

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“…As expected from its A-T specificity (45,52), netropsin reduces quinacrine fluorescence without, however, displacing it from calf thymus DNA (Fig. 7A), consistent with a relocation of the quinacrine from A-T rich sites to sites conferring a lower quantum yield.…”

Section: Resultssupporting

confidence: 80%

Interactions between pairs of DNA‐binding dyes: Results and implications for chromosome analysis

et al. 1980

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A number of DNA-binding dyes, with spectral properties making them suitable as components of energy donor-acceptor pairs, are described. If such pairs are used to stain metaphase chromosomes, and if the energy acceptor (e.g., actinomycin D or methyl green) has a binding specificity opposite to the binding or fluorescence specificity of the donor (e.g,, 33258 Hoechst, quinacrine or chromomycin A3), contrast in donor fluorescence can be enhanced, leading to patterns selectively highlighting standard or reverse chromosome bands or particular polymorphic regions. Such results presumably reflect chromosomal regions enriched in 10-20 base pair clusters to which the donor binds and fluoresces but to which the acceptor cannot bind. For other pairs, involving counterstains such as netropsin or echinomycin, which are not suitable as energy acceptors, specific changes observed in polymorphic region fluorescence are most likely due to binding competition between dyes. Dye pairs producing contrast by either method can be used to differentiate between homologous chromosomes or to facilitate detection of specific chromosomal rearrangements. Preliminary data indicate that contrast enhancement generated in fixed metaphase chromosomes spread on microscopic slides can also be observed in suspensions of unfixed metaphase chromosomes, reinforcing the expectation that the methodology described will be of use in flow cytometry.Key terms: Energy transfer, fluorescence, binding competition, chromosome banding patterns, polymorphisms, rearrangements, flow cytometry.Staining metaphase chromosomes simultaneously with pairs of different dyes can lead t o new fluorescence patterns. In addition to the signals produced when the dyes are used independently, information can be generated by interactions between these dyes. For example, two dyes can compete for binding to certain chromosomal sites, which can thereby be stained differentially (15,41) Alternatively, indirect effects of one dye on another can be mediated via conformational changes induced in DNA (46). In addition, because of a coincidence between the range of separations possible between ' Supported by Grant GM21121 from the National Institutes of Health. S.A.L. is the recipient of a Research Career Development Award GM00122 from the National Institute of General Medical Sciences and E.S. is supported in part by a grant from the Whitaker Foundation.* Presented in part at Automated Cytology VII, Asilomar, California, November 25-30, 1979. dye molecules bound to DNA (20) and the effective distance over which dye electronic transition dipoles can interact (typically 5 50 A) (9, 42), the transfer of electronic excitation energy from one dye to another in doubly stained chromatin can be appreciable (14,16,17,36).We have recently shown that the enhanced contrast in metaphase chromosome staining produced by certain dye pairs is due largely to energy transfer, while that produced by other pairs, which fail to satisfy spectral overlap criteria, is due primarily to binding competition (37)....

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“…It exhibits antiviral, antifungal, and antibacterial activities and inhibits DNA and RNA tumor viruses in mammalian cells (2). Netropsin complexes with duplex DNA but does not complex with single-stranded DNA, double-stranded RNA, or DNA-RNA hybrids (3,4). DNA and RNA synthesis is inhibited following netropsin interaction with the template and/or primer nucleic acid duplex (4,5).…”

mentioning

confidence: 99%

“…Studies on a series of synthetic polynucleotides demonstrate the presence of one major binding site with the netropsin molecule spanning from three to five base pairs (7)(8)(9). Netropsin complexes to synthetic DNAs containing dA-dT, dA-dBrU, dI-dC, and dI-dBrC base pairs but not to synthetic DNAs containing dG-dC base pairs (3,4). This suggests that netropsin binds in the minor groove and that the 2-amino group of guanine inhibits complex formation (4).…”

mentioning

confidence: 99%

Netropsin-poly(dA-dT) complex in solution: structure and dynamics of antibiotic-free base pair regions and those centered on bound netropsin.

Patel¹,

Canuel²

1977

Proc. Natl. Acad. Sci. U.S.A.

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The biphasic duplex-to-strand transition for the netropsin-poly(dA-dT) complex, phosphate/drug mole ratio (P/D) = 50, has been investigated by high-resolution proton nuclear magnetic resonance (NMR) spectroscopy at the nonexchangeable base and sugar protons in 0.1 M cacodylate solution. The NMR spectral parameters monitor the structure and dynamics of thle opening of antibiotic-free base pair regions Netropsin is a basic oligopeptide isolated from Streptomyces netropsis which is composed of 1-methylpyrrole-2-carboxamide moieties linked to guanidinoacetamidino and amidinopropyl groups ( Fig. 1) (1). It exhibits antiviral, antifungal, and antibacterial activities and inhibits DNA and RNA tumor viruses in mammalian cells (2). Netropsin complexes with duplex DNA but does not complex with single-stranded DNA, double-stranded RNA, or DNA-RNA hybrids (3,4). DNA and RNA synthesis is inhibited following netropsin interaction with the template and/or primer nucleic acid duplex (4, 5). Netropsin neither intercalates nor unwinds the DNA double helix (4, 6). Studies on a series of synthetic polynucleotides demonstrate the presence of one major binding site with the netropsin molecule spanning from three to five base pairs (7-9). Netropsin complexes to synthetic DNAs containing dA-dT, dA-dBrU, dI-dC, and dI-dBrC base pairs but not to synthetic DNAs containing dG-dC base pairs (3, 4). This suggests that netropsin binds in the minor groove and that the 2-amino group of guanine inhibits complex formation (4). Models for the netropsin-DNA complex stress the importance of electrostatic interactions between the charged ends of the antibiotic and the backbone phosphates and the contributions from peptide-The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked NMR Spectra. Proton NMR spectra were recorded in the Fourier transform mode on a Bruker HX-360 NMR spectrometer interfaced to a Nicolet BNC-12 computer. The chemical shifts are referenced relative to internal standard, 2,2-dimethyl-2-silapentane-5-sulfonate (DSS). The temperature of the probe was calibrated to ±1 using ethyleneglycol.Ultraviolet-Visible Spectra. Optical studies were undertaken on samples (0.25 cm3 volume) placed in water-jacketed 1-mm path length cylindrical Helma cells with Teflon caps, and the UV-visible absorbance data were recorded on a Cary 118 C spectrometer. Automatic stepwise increases in temperature of 10/min followed by a dwell time of 4 min were maintained by a TP2 programmer attached to a RTE-8 Neslab circulating bath. An immersible microprobe (Bailey IT-1 implantable, 18 gauge) was put into the reference solution through a bore in the Teflon cap and the temperature was monitored by a digital thermometer (Bailey BAT-8). The nucleic acid 260-and 278-nm absorbance values were read directly on the digital readout of the Cary 118 C following zeroing of the baseline at 700 nm at each temperature.Abbreviations: NMR, nuclear magnetic resonance; P/D, phosphate/ dr...

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Interaction of the oligopeptide antibiotics netropsin and distamycin a with nucleic acids

Cited by 170 publications

References 36 publications

Evidence of the differentiated structural arrangement of constitutive heterochromatin between two populations of Astyanax scabripinnis (Pisces, Characidae)

Evidence of the differentiated structural arrangement of constitutive heterochromatin between two populations of Astyanax scabripinnis (Pisces, Characidae)

Interactions between pairs of DNA‐binding dyes: Results and implications for chromosome analysis

Netropsin-poly(dA-dT) complex in solution: structure and dynamics of antibiotic-free base pair regions and those centered on bound netropsin.

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