Feb 7, 2020

PICH translocase activity is required for proper distribution of SUMOylated proteins on mitotic chromosomes

Victoria A HassebroekYoshiaki Azuma


Polo-like kinase interacting checkpoint helicase (PICH) is a SNF2 family DNA translocase and is a Small Ubiquitin-like modifier (SUMO) binding protein. Despite that both translocase activity and SUMO-binding ability are required for proper chromosome segregation, how these two activities function to mediate chromosome segregation remains unknown. Here, we show that PICH specifically promotes redistribution of SUMOylated proteins like SUMOylated TopoisomeraseIIα (TopoIIα) on mitotic chromosomes. Conditional depletion of PICH using the Auxin Inducible Degron (AID) system resulted in the retention of SUMOylated chromosomal proteins, including TopoIIα, indicating that PICH functions to redistribute these proteins. Replacement of endogenous PICH with exogenous PICH mutants showed that PICH translocase activity is required for SUMOylated protein redistribution. In vitro assays showed that PICH specifically regulates SUMOylated TopoIIα activity using its SUMO-binding ability. Taken together, we propose a novel function of PICH in remodeling SUMOylated chromosomal proteins to ensure faithful chromosome segregation.

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Mentioned in this Paper

ERCC6L protein, human
Pharmacologic Substance
IAA12 protein, Arabidopsis
Ubiquitin-Like Proteins
Chromosome Segregation
SMARCA4 protein, human

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