Comparative studies of the binding of ethidium bromide and its photoreactive analogs to nucleic acids by fluorescence and rapid kinetics

Garland, Frank C.; Graves, David E.; Yielding, Lerena W.; Cheung, Herbert C.

doi:10.1021/bi00555a019

Biochemistry

1980

DOI: 10.1021/bi00555a019

|View full text |Cite

Comparative studies of the binding of ethidium bromide and its photoreactive analogs to nucleic acids by fluorescence and rapid kinetics

Frank C. Garland¹,

David E. Graves²,

Lerena W. Yielding³

et al.

Abstract: The binding studies of the interaction of ethidium bromide with DNA have been hampered by its reversibility, which prevents direct isolation and thus characterization of the complex. The recent development of photoaffinity labeling has provided a means to circumvent this problem. However, to be useful as a probe for the parent compound, a photosensitive analogue must be shown to interact in vivo and in vitro just as the parent analogue. These studies demonstrate by steady-state and nonosecond fluorescence and … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

1982

2007

Publication Types

Select...

Article8

Relationship

Self Cite2

Independent6

Authors

Journals

Cited by 60 publications

(23 citation statements)

References 27 publications

(17 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To distinguish between these two possibilities, the lifetime of the, probe incorporated into both untreated and treated cells was determined in a photon-counting PRA 2000 pulse nanosecond fluorimeter using 339 nm for excitation and a Coming 3-73 cutofffilter to isolate the emission. The decay data were analyzed as described (27). Two lifetimes were detected with both samples, one in the range 3-4 nsec and the other around 9 nsec.…”

mentioning

confidence: 99%

Interferon inhibits Sendai virus-induced cell fusion: an effect on cell membrane fluidity.

Chatterjee¹,

Cheung²,

Hunter³

1982

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

View full text Add to dashboard Cite

Interferon can affect several cellular functions, in addition to its antiviral activity. We report here that pretreatment of human cells with homologous interferon significantly inhibits cell fusion induced by Sendai virus and that this refractory state is accompanied by a decrease in cell plasma membrane fluidity. Multinucleate cell formation induced by 13-propiolactone-inactivated Sendai virus in human fibroblast cells (a system in which fusion results from an interaction ofthe viral glycoprotein with the cell membrane) was inhibited by more than 90% after addition of human interferon for [18][19][20][21][22][23][24] hr. This inhibition could be neutralized by antiserum to interferon. Furthermore, inhibitor studies with cycloheximide and actinomycin D clearly indicated that synthesis of protein and RNA is necessary to establish the resistant state. To determine whether the inhibition of Sendai virus-induced cell fusion resulted from interferon-induced changes at the cell plasma membrane, experiments were carried out using the fluorescence probe 1,6-diphenyl-1,3,5-hexatriene, which is capable of sensing molecular motions in the hydrocarbon core of the bilayer structure. A significant decrease in the membrane fluidity of interferon-treated cells was observed. It is likely, therefore, that the inhibitory effect on Sendai virus-induced cell fusion observed in interferon-treated cells results from an increased rigidity of the target cell membrane.In addition to their potent antiviral action, interferons (IFNs) have various effects on normal cellular functions. It can bind to specific receptors in the plasma membrane of normal and transformed cells and regulate both their motility (1, 2), and their rates of growth and division (3, 4). IFN treatment has also been shown to alter both plasma membrane density and the concentrations of some plasma membrane glycoproteins (5-7). Furthermore, it is known that IFN plays an important role in modulating the immune response of a host to infection (8, 9). It is clear that many of these changes induced by IFN could be mediated by alterations in membrane-associated functions of the treated cell.We showed previously that pretreatment of cells with homologous IFN reduced the number as well as the size of multinucleate cells induced after infection with the type D retrovirus M-PMV (10). These results were consistent with our findings that cell fusion induced by M-PMV and two other type D retroviruses required penetration of the cell by the virus and translation of virus-associated RNA (11,12). Studies from several laboratories had indicated that translation of viral mRNA could be severely inhibited in IFN-treated cells (reviewed in refs. 13 and 14). This inhibition appears to occur via two discrete pathways: the first involves phosphorylation of eukaryotic initiation factor 2 which might prevent the binding oftRNA to 40S ribosomal subunits (15), and the second is through a 2',5' Adependent endonuclease which is activated in IFN-treated cells (16,17).Despite the fact that the...

show abstract

mentioning

confidence: 99%

Interferon inhibits Sendai virus-induced cell fusion: an effect on cell membrane fluidity.

Chatterjee¹,

Cheung²,

Hunter³

1982

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

View full text Add to dashboard Cite

show abstract

“…were stored at 48, and were used within one week. The concentration of EB was determined spectrophotometrically at 480 nm (e ¼ 5,680 m À 1 cm À 1 ) [70]. 3.2.…”

mentioning

confidence: 99%

Mixed‐Ligand Copper(II)–Phenanthroline–Dipeptide Complexes: Synthesis, Characterization, and DNA‐Cleavage Properties

Reddy

Pallerla

2007

Chemistry & Biodiversity

View full text Add to dashboard Cite

The mixed-ligand complexes [Cu(II)(HisLeu)(phen)](+) (1) and [Cu(II)(HisSer)(phen)](+) (2; phen=1,10-phenanthroline) were synthesized and characterized. The intercalative interaction of the Cu(II) complexes with calf-thymus DNA (CT-DNA) was probed by UV/VIS and fluorescence titration, as well as by thermal-denaturation experiments, and the intrinsic binding constants (K(b)) for the complexes with 1 and 2 were 4.2x10(3) and 4.9x10(3) M(-1), resp. Both complexes were found to be efficient catalysts for the hydrolytic cleavage of plasmid pUC19 DNA, as tested by gel electrophoresis, converting the DNA from the supercoiled to the nicked-circular form at rate constants of 1.32 and 1.40 h(-1) for 1 and 2, resp.

show abstract

“…Double-distilled, salt-free H 2 O was used to prepare all solns. The concentration of ETB was determined spectrophotometrically, using an e value of 5680 m À1 cm À1 at 480 nm [36]. 2.…”

mentioning

confidence: 99%

Ternary Zinc(II)-Dipeptide Complexes for the Hydrolytic Cleavage of DNA at Physiological pH

Reddy

Mohan

Rao

2005

C&B

View full text Add to dashboard Cite

A series of Zn(II) complexes with cysteinylglycine (CysGly) and histidylserine (HisSer), and of CysGly and histidylphenylalanine (HisPhe) were investigated. Complex stabilities were determined potentiometrically, and binding geometries were probed by means of 1H-NMR spectroscopy, using Co(II) instead of Zn(II) as a spectroscopic marker. The ternary 1:1:1 complexes [Zn(II)(CysGly)(HisSer)] and [Zn(II)(CysGly)(HisPhe)] were shown by UV experiments, fluorescence titration, and gel electrophoresis to intercalate with DNA, and to hydrolytically cleave supercoiled DNA (form-I), partly also circular (form-II) DNA, under physiological conditions (37 degrees, H2O, pH 7.5).

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

hi@scite.ai

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Comparative studies of the binding of ethidium bromide and its photoreactive analogs to nucleic acids by fluorescence and rapid kinetics

Cited by 60 publications

References 27 publications

Interferon inhibits Sendai virus-induced cell fusion: an effect on cell membrane fluidity.

Interferon inhibits Sendai virus-induced cell fusion: an effect on cell membrane fluidity.

Mixed‐Ligand Copper(II)–Phenanthroline–Dipeptide Complexes: Synthesis, Characterization, and DNA‐Cleavage Properties

Ternary Zinc(II)-Dipeptide Complexes for the Hydrolytic Cleavage of DNA at Physiological pH

Contact Info

Product

Resources

About