Abstract
Accessibility of linker-DNA chromatin during salt-induced condensation of chicken erythrocytes chromatin was studied by diffusion-enhanced resonance energy transfer. A terbium complex was covalently bound to linker-DNA and fluorescein molecules bound to latex particles with diameters ranging from 14 to 2470 nm were used as acceptor. The accessibility of linker-DNA to molecules with a diameter superior to 14 nm diminished during condensation, but for an acceptor diameter of 14 nm or less, no accessibility variation was observed. It can be concluded that (1) linker-DNA is located inside the fiber when chromatin is in the condensed state, (2) chromatin condensation can prevent the approach to DNA due to steric hindrance, (3) salt-induced chromatin condensation is a gradual process, and (4) condensed chromatin models containing a central cavity are more likely.
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Abbreviations
- DTPA:
-
diethylene tetramine pentacetic acid
- FDL-DERET:
-
fast diffusion limit of diffusion-enhanced resonance energy transfer
- Pso-Tb:
-
psoralen-terbium complex
- PAS:
-
paraamino salicylic acid
- TREF:
-
time-resolved emission of fluorescence
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Labarbe, R., Mignon, S., Flock, S. et al. Diffusion-enhanced resonance energy transfer shows that linker-DNA accessibility decreases during salt-induced chromatin condensation. J Fluoresc 6, 107–118 (1996). https://doi.org/10.1007/BF00732050
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DOI: https://doi.org/10.1007/BF00732050