ArticleResearch square2026
Structural basis of condensin II activation.
Article in Research square, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
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Authors and funding
5 authors.
Funding
Abstract
Condensin II is present in the nucleus throughout interphase, yet does not acquire robust loop-extruding activity until cells enter prophase. How the complex is kept inactive before prophase has remained unclear. Here we show, by cryo-EM and mass photometry, that nucleotide-free human condensin II forms a reversible dimer at physiological ionic strength. In this dimer, CAP-H2 elements required for chromosome association are buried, while the C-terminal tail of CAP-D3 holds the neck gate open by blocking engagement of the CAP-H2 neck-binding domain with the SMC2 neck. Nucleotide binding promotes monomerization and causes the SMC module to rotate toward the displaced neck-binding domain, but persistent CAP-D3 blockade keeps the gate open. These structures explain CAP-D3-dependent self-suppression of condensin II activity and suggest how nucleotide binding and M18BP1 engagement promote progression from an autoinhibited state toward a poised, pre-clamping intermediate.
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Registered trials
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