Nucleosome-remodelling machines and other molecular motors observed at the single-molecule level.

Publication Type:

Journal Article

Source:

The FEBS journal, Volume 278, Issue 19, p.3596-607 (2011)

DOI:

10.1111/j.1742-4658.2011.08280.x

Keywords:

Adenosine Triphosphatases; Chromatin; Chromatin Assembly and Disassembly; DNA; Microscopy, Atomic Force; Microscopy, Electron, Transmission; Molecular Motor Proteins; Nucleic Acid Conformation; Nucleosomes; OPTICAL TWEEZERS

Abstract:

Through its capability to transiently pack and unpack our genome, chromatin is a key player in the regulation of gene expression. Single-molecule approaches have recently complemented conventional biochemical and biophysical techniques to decipher the complex mechanisms ruling chromatin dynamics. Micromanipulations with tweezers (magnetic or optical) and imaging with molecular microscopy (electron or atomic force) have indeed provided opportunities to handle and visualize single molecules, and to measure the forces and torques produced by molecular motors, along with their effects on DNA or nucleosomal templates. By giving access to dynamic events that tend to be blurred in traditional biochemical bulk experiments, these techniques provide critical information regarding the mechanisms underlying the regulation of gene activation and deactivation by nucleosome and chromatin structural changes. This minireview describes some single-molecule approaches to the study of ATP-consuming molecular motors acting on DNA, with applications to the case of nucleosome-remodelling machines.

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