1. ACF Takes the Driver’s Seat
Hari R. Singh, Andreas G. Ladurner 
Molecular Cell 
Volume 55, Issue 3, Pages (August 2014)
DOI: /j.molcel
Copyright © 2014 Elsevier Inc. Terms and Conditions

2. Figure 1
Regulatory Domains within the ACF-Nucleosome Complex Act as a Gas Pedal or Brake on Sliding Activity
(A) Domain architecture of the ACF complex subunits. Catalytic Snf2h with the regulatory AutoN and NegC motifs and the N-terminal domain of Acf1, which Hwang et al. (2014) find to be important for gauging linker DNA length.
(B) Working model for the linker DNA length-dependent activity of ACF. The Acf1 N-terminal domain switches between binding linker DNA (when the linker is long) or the histone H4 tail (when linker is short). This determines whether the regulatory AutoN domain of Snf2h contacts and inhibits the ATPase domain (adapted from Hwang et al., 2014).
Molecular Cell  , DOI: ( /j.molcel )
Copyright © 2014 Elsevier Inc. Terms and Conditions