RSC remodeling of oligo-nucleosomes: an atomic force microscopy study.

Fabien Montel, Martin Castelnovo, Hervé Menoni, Dimitar Angelov, Stefan Dimitrov, Cendrine Faivre-Moskalenko

Université de Lyon, Laboratoire de Physique, CNRS UMR 5672, Lyon Cedex 07, France.

Nucleic acids research 2011 Apr

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The 'remodels structure of chromatin' (RSC) complex is an essential chromatin remodeling factor that is required for the control of several processes including transcription, repair and replication. The ability of RSC to relocate centrally positioned mononucleosomes at the end of nucleosomal DNA is firmly established, but the data on RSC action on oligo-nucleosomal templates remains still scarce. By using atomic force microscopy (AFM) imaging, we have quantitatively studied the RSC-induced mobilization of positioned di- and trinucleosomes as well as the directionality of mobilization on mononucleosomal template labeled at one end with streptavidin. AFM imaging showed only a limited set of distinct configurational states for the remodeling products. No stepwise or preferred directionality of the nucleosome motion was observed. Analysis of the corresponding reaction pathways allows deciphering the mechanistic features of RSC-induced nucleosome relocation. The final outcome of RSC remodeling of oligosome templates is the packing of the nucleosomes at the edge of the template, providing large stretches of DNA depleted of nucleosomes. This feature of RSC may be used by the cell to overcome the barrier imposed by the presence of nucleosomes.

Citation

Fabien Montel, Martin Castelnovo, Hervé Menoni, Dimitar Angelov, Stefan Dimitrov, Cendrine Faivre-Moskalenko. RSC remodeling of oligo-nucleosomes: an atomic force microscopy study. Nucleic acids research. 2011 Apr;39(7):2571-9