Cohesin is a ring-shaped protein complex that plays a crucial role in sister 
chromatid cohesion and gene expression. The dynamic association of cohesin with 
chromatin is essential for these functions. However, the exact nature of cohesin 
dynamics, particularly cohesin translocation, remains unclear. We evaluated the 
dynamics of individual cohesin molecules on DNA and found that the cohesin core 
complex possesses an intrinsic ability to traverse DNA in an adenosine 
triphosphatase (ATPase)-dependent manner. Translocation ability is suppressed in 
the presence of Wapl-Pds5 and Sororin; this suppression is alleviated by the 
acetylation of cohesin and the action of mitotic kinases. In Xenopus laevis egg 
extracts, cohesin is translocated on unreplicated DNA in an ATPase- and Smc3 
acetylation-dependent manner. Cohesin movement changes from bidirectional to 
unidirectional when cohesin faces DNA replication; otherwise, it is incorporated 
into replicating DNA without being translocated or is dissociated from 
replicating DNA This study provides insight into the nature of individual 
cohesin dynamics and the mechanisms by which cohesin achieves cohesion in 
different chromatin contexts.