Aggregation and fusion of lipid vesicles induced by diphtheria toxin at low pH: Possible involvement of the P site and the NAD+ binding site

1985 ◽  
Vol 5 (3) ◽  
pp. 243-250 ◽  
Author(s):  
Veronique Cabiaux ◽  
Michel Vandenbranden ◽  
Paul Falmagne ◽  
Jean-Marie Ruysschaert
Keyword(s):  
Energy Transfer ◽  
Binding Site ◽  
Fluorescent Probes ◽  
Diphtheria Toxin ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Lipid Vesicles ◽  
Low Ph ◽  
Model Membranes

Model membranes have been used to study the interaction between diphtheria toxin and lipids. We report here on the ability of this toxin to induc% at low pH, fusion and aggregation of asolectin lipid vesicles. Resonance energy transfer experiments using lipid fluorescent probes make it possible to discriminate between these two processes.

scholarly journals Resonance energy transfer microscopy: observations of membrane-bound fluorescent probes in model membranes and in living cells.

1986 ◽  
Vol 103 (4) ◽  
pp. 1221-1234 ◽  
Author(s):  
P S Uster ◽  
R E Pagano
Keyword(s):  
Energy Transfer ◽  
Fluorescent Probes ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Living Cells ◽  
Model Membranes ◽  
Energy Donor ◽  
Membrane Bound ◽  
Energy Acceptor ◽  
In Cells

A conventional fluorescence microscope was modified to observe the sites of resonance energy transfer (RET) between fluorescent probes in model membranes and in living cells. These modifications, and the parameters necessary to observe RET between membrane-bound fluorochromes, are detailed for a system that uses N-4-nitrobenzo-2-oxa-1,3-diazole (NBD) or fluorescein as the energy donor and sulforhodamine as the energy acceptor. The necessary parameters for RET in this system were first optimized using liposomes. Both quenching of the energy donor and sensitized fluorescence of the energy acceptor could be directly observed in the microscope. RET microscopy was then used in cultured fibroblasts to identify those intracellular organelles labeled by the lipid probe, N-SRh-decylamine (N-SRh-C10). This was done by observing the sites of RET in cells doubly labeled with N-SRh-C10 and an NBD-labeled lipid previously shown to label the endoplasmic reticulum, mitochondria, and nuclear envelope. RET microscopy was also used in cells treated with fluorescein-labeled Lens culinaris agglutinin and a sulforhodamine derivative of phosphatidylcholine to examine the internalization of plasma membrane lipid and protein probes. After internalization, the fluorescent lectin resided in most, but not all of the intracellular compartments labeled by the fluorescent lipid, suggesting sorting of the membrane-bound lectin into a subset of internal compartments. We conclude that RET microscopy can co-localize different membrane-bound components at high resolution, and may be particularly useful in examining temporal and spatial changes in the distribution of fluorescent molecules in membranes of the living cell.

scholarly journals Multicolor protein FRET with tryptophan, selective coumarin-cysteine labeling, and genetic acridonylalanine encoding

2017 ◽  
Vol 53 (80) ◽  
pp. 11072-11075 ◽  
Author(s):  
John J. Ferrie ◽  
Naoya Ieda ◽  
Conor M. Haney ◽  
Christopher R. Walters ◽  
Itthipol Sungwienwong ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Fluorescent Probes ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Forster Resonance Energy Transfer ◽  
Förster Resonance Energy Transfer ◽  
Site Specific ◽  
Cysteine Labeling ◽  
Förster Resonance

A combination of labeling techniques enables site-specific installation of fluorescent probes for measuring distances within proteins by Förster resonance energy transfer (FRET).

Location of the stilbenedisulfonate binding site of the human erythrocyte anion-exchange system by resonance energy transfer

Biochemistry ◽  
1979 ◽  
Vol 18 (21) ◽  
pp. 4505-4516 ◽  
Author(s):  
Anjana Rao ◽  
Paul Martin ◽  
Reinhart A. F. Reithmeier ◽  
Lewis C. Cantley
Keyword(s):  
Energy Transfer ◽  
Binding Site ◽  
Anion Exchange ◽  
Human Erythrocyte ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Exchange System

Location of Novel Benzanthrone Dyes in Model Membranes as Revealed by Resonance Energy Transfer

2014 ◽  
Vol 24 (3) ◽  
pp. 899-907 ◽  
Author(s):  
Olga Zhytniakivska ◽  
Valeriya Trusova ◽  
Galyna Gorbenko ◽  
Elena Kirilova ◽  
Inta Kalnina ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Model Membranes ◽  
Benzanthrone Dyes
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