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Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging
Published on: January 31, 2019
RSC remodeling of oligo-nucleosomes: an atomic force microscopy study
Fabien Montel1, Martin Castelnovo, Hervé Menoni
1Université de Lyon, Laboratoire de Physique, CNRS UMR 5672, Lyon Cedex 07, France.
Nucleic Acids Research
|December 9, 2010
Summary
The
Area of Science:
- Chromatin biology
- Molecular mechanisms of DNA processes
Background:
- The 'remodels structure of chromatin' (RSC) complex is crucial for DNA processes like transcription, repair, and replication.
- While RSC's action on single nucleosomes is known, its effects on multiple nucleosomes (oligosomes) are less understood.
Purpose of the Study:
- To quantitatively investigate the RSC complex's mobilization of di- and trinucleosomes using atomic force microscopy (AFM).
- To determine the directionality of nucleosome movement induced by RSC on specifically labeled mononucleosomal templates.
Main Methods:
- Utilized atomic force microscopy (AFM) for high-resolution imaging of nucleosome dynamics.
- Employed quantitative analysis of RSC-induced nucleosome mobilization on di- and trinucleosomal templates.
- Studied directionality using mononucleosomal templates labeled with streptavidin.
Main Results:
- AFM imaging revealed a limited number of distinct structural states after RSC remodeling.
- No stepwise or directional preference was observed in nucleosome movement.
- RSC remodeling of oligosomes resulted in nucleosome packing at the template edge, exposing DNA.
Conclusions:
- RSC remodeling of oligosomes leads to nucleosome eviction, creating accessible DNA regions.
- This mechanism may enable cells to overcome nucleosomal barriers during essential DNA processes.
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