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Cohesin ATPase activities regulate DNA binding and coiled-coil configuration by Xingya Xu; Ryuta Kanai; Li Wang; Mitsuhiro Yanagida is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Significance Cohesin is a heteropentameric protein complex consisting of two structural maintenance of chromosomes (SMC) subunits and three non-SMC subunits. The two SMC subunits form a heterodimer with an ATPase head and hinge that are connected by long coiled coils. Isolation of ATPase mutants followed by comprehensive identification of suppressor mutations in SMC subunits that can bypass ATPase defects was performed. Locations and properties of mutant alleles reflect how ATPase activities could be compromised by structural adaptation. ATP-driven conformational changes may enhance DNA anchoring by the head, alter interactions of coiled coils at the head with other subunits for DNA to go through, and fold/extend coiled coils near break sites around midpoint to bring together DNA elements far from each other.

Who reads Cohesin ATPase activities regulate DNA binding and coiled-coil configuration?

Author

Xingya Xu; Ryuta Kanai; Li Wang; Mitsuhiro Yanagida

Publisher

Proceedings of the National Academy of Sciences

Published

2022

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)