Gradual opening of Smc arms in prokaryotic condensin
Multi-subunit SMC ATPases control chromosome superstructure apparently by catalyzing a DNA-loop-extrusion reaction. SMC proteins harbor an ABC-type ATPase head and a hinge dimerization domain connected by a coiled coil arm. Two arms in a SMC dimer can co-align, thereby forming a rod-shaped particle. Upon ATP binding, SMC heads engage, and arms are thought to separate. Here, we studied the shape of B. subtilis Smc-ScpAB by electron-spin resonance spectroscopy. Arm separation was readily detected proximal to the heads in the absence of ligands, while separation near the hinge largely depended on ATP and DNA. Artificial blockage of arm opening eliminated DNA stimulation of ATP hydrolysis, but did not prevent basal ATPase activity. We identified an arm-to-arm contact as being important for controlling the molecular transformations. Point mutations at this arm interface eliminate Smc function. We propose that partially open, intermediary conformations provide directionality to SMC DNA translocation by binding suitable DNA substrates.