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Condensin chromatin association is regulated by the combined actions of SMC head and hinge engagement and phosphorylation

ABSTRACT: The SMC condensin complex is essential for normal mitotic chromosome structure in eukaryotes. Here we undertake a comprehensive analysis of the importance of the condensin ATP binding and hydrolysis, SMC hinge stability and condensin subunit phosphorylation for chromatin association in budding yeast. We demonstrate that ATP binding is required for condensin chromatin association by both promoting stable binding of Smc4 and enabling head-head engagement. In contrast destabilizing the hinge domain of condensin facilitates chromatin association. Phosphorylation of condensin is enriched in enzymatic states with elevated chromatin association. Furthermore, condensin phosphorylation and Aurora/Ipl1 kinase function are required to maintain mitotic chromatin association. We find that Ipl1 activity stabilizes Smc4 interaction within the complex in a similar manner to ATP binding, illustrating a novel pathway of regulation of condensin activity by phosphorylation. In summary condensin’s chromatin association is positively regulated by phosphorylation and SMC ATP binding dependent head engagement and negatively regulated by hinge engagement. Our data argues that control of chromatin association by phosphorylation is through regulation of specific steps of its enzymatic cycle.

INSTRUMENT(S):

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Steve Sweet

LAB HEAD: Jon Baxter

PROVIDER: PXD006028 | Pride | 2025-10-14

REPOSITORIES: Pride

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			Action	DRS
	150120_SMC2-wt_100_NOCO.RAW	Raw
	150120_SMC2-wt_130DOWN_NOCO.RAW	Raw
	150120_SMC2-wt_130MIDDLE_NOCO.RAW	Raw
	150120_SMC2-wt_130UP_NOCO.RAW	Raw
	150120_SMC2-wt_200DOWN_NOCO.RAW	Raw

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