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EMBO J. 2016 Dec 15;35(24):2686-2698. Epub 2016 Nov 21.

Cohesin acetylation and Wapl-Pds5 oppositely regulate translocation of cohesin along DNA.

Author information

1
Division of Biological Science, Graduate School of Science Nagoya University, Nagoya, Japan.
2
Research Institute of Molecular Pathology, Vienna, Austria.
3
Division of Biological Science, Graduate School of Science Nagoya University, Nagoya, Japan nishiyama@bio.nagoya-u.ac.jp.

Abstract

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.

KEYWORDS:

DNA replication; chromosome segregation; cohesin; post‐translational modification; single‐molecule TIRF microscopy

PMID:
27872142
PMCID:
PMC5167340
DOI:
10.15252/embj.201695756
[Indexed for MEDLINE]
Free PMC Article

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