Electron microscopy studies of nucleosome remodelers

ATP-dependent chromatin remodeling complexes, or remodelers, are large protein assemblies that use the energy from ATP hydrolysis to non-covalently modify the structure of nucleosomes, playing a central role in the regulation of chromatin dynamics. Our understanding of the mechanism and regulation of this remodeling activity and the diversity of products that chromatin remodelers can generate remains limited, partly because very little structural data are available on these challenging samples. Electron microscopy (EM) and single-particle approaches have made inroads into the structural characterization of a number of remodeling complexes. Here I will review the work done to date, focusing on functional insights we have gained from these structures.

► Remodelers are large protein complexes that modify the structure of nucleosomes.
► Electron microscopy (EM) has provided the only structures of full remodelers.
► EM reconstructions have provided insights into nucleosome-binding sites.
► EM reconstructions have provided insights into remodeling mechanisms.