Atomic Force Microscopy Imaging of SWI/SNF Action: Mapping the Nucleosome Remodeling and Sliding

@article{citeulike:1412894, abstract = {We propose a combined experimental (atomic force microscopy) and theoretical study of the structural and dynamical properties of nucleosomes. In contrast to biochemical approaches, this method allows us to determine simultaneously the DNA-complexed length distribution and nucleosome position in various contexts. First, we show that differences in the nucleoproteic structure observed between conventional H2A and H2A.Bbd variant nucleosomes induce quantitative changes in the length distribution of DNA-complexed with histones. Then, the sliding action of remodeling complex SWI/SNF is characterized through the evolution of the nucleosome position and wrapped DNA length mapping. Using a linear energetic model for the distribution of DNA-complexed length, we extract the net-wrapping energy of DNA onto the histone octamer and compare it to previous studies. 10.1529/biophysj.107.105569}, author = {Montel, Fabien and Fontaine, Emeline and St-Jean, Philippe and Castelnovo, Martin and Faivre-Moskalenko, Cendrine }, citeulike-article-id = {1412894}, doi = {http://dx.doi.org/10.1529/biophysj.107.105569}, journal = {Biophys. J.}, keywords = {afm, biophysics, chromatin, mapping, nucleosomes}, month = {July}, number = {2}, pages = {566--578}, posted-at = {2007-06-26 06:14:06}, priority = {3}, title = {Atomic Force Microscopy Imaging of SWI/SNF Action: Mapping the Nucleosome Remodeling and Sliding}, url = {http://dx.doi.org/10.1529/biophysj.107.105569}, volume = {93}, year = {2007} }

TY - JOUR ID - citeulike:1412894 L3 - citeulike-article-id:1412894 TI - Atomic Force Microscopy Imaging of SWI/SNF Action: Mapping the Nucleosome Remodeling and Sliding JF - Biophys. J. VL - 93 IS - 2 SP - 566 EP - 578 N2 - We propose a combined experimental (atomic force microscopy) and theoretical study of the structural and dynamical properties of nucleosomes. In contrast to biochemical approaches, this method allows us to determine simultaneously the DNA-complexed length distribution and nucleosome position in various contexts. First, we show that differences in the nucleoproteic structure observed between conventional H2A and H2A.Bbd variant nucleosomes induce quantitative changes in the length distribution of DNA-complexed with histones. Then, the sliding action of remodeling complex SWI/SNF is characterized through the evolution of the nucleosome position and wrapped DNA length mapping. Using a linear energetic model for the distribution of DNA-complexed length, we extract the net-wrapping energy of DNA onto the histone octamer and compare it to previous studies. 10.1529/biophysj.107.105569 KW - afm KW - biophysics KW - chromatin KW - mapping KW - nucleosomes AU - Montel, Fabien AU - Fontaine, Emeline AU - St-Jean, Philippe AU - Castelnovo, Martin AU - Faivre-Moskalenko, Cendrine PY - 2007/07/15/ UR - http://dx.doi.org/10.1529/biophysj.107.105569 ER -