Mechanisms for ATP-dependent chromatin remodelling: The means to the end

Chromatin remodelling is the ATP-dependent change in nucleosome organisation driven by Snf2 family ATPases. The biochemistry of this process depends on the behaviours of ATP-dependent motor proteins and their dynamic nucleosome substrates, which brings significant technical and conceptual challenges. Steady progress has been made in characterising the polypeptides of which these enzymes are comprised. Divergence in the sequences of different subfamilies of Snf2-related proteins suggests that the motors are adapted for different functions. Recently, structural insights have suggested that the Snf2 ATPase acts as a context-sensitive DNA translocase. This may have arisen as a means to enable efficient access to DNA in the high density of the eukaryotic nucleus. How the enzymes engage nucleosomes and how the network of noncovalent interactions within the nucleosome respond to the force applied remains unclear, and it remains prudent to recognise the potential for both DNA distortions and dynamics within the underlying histone octamer structure. The biochemistry of chromatin remodelling depends on ATP dependent motor proteins and their dynamic nucleosome substrates. Recent structural insights suggests the Snf2 ATPase is a context-sensitive DNA translocase which may have arisen to enable efficient access to DNA in the high density of the eukaryotic nucleus. How the enzymes engage nucleosomes and induce changes within the nucleosome still remains unclear.