ReviewFrontiers in molecular biosciences2026
Structural and mechanistic perspectives on Nse5/6 regulation of the Smc5/6 complex.
Review in Frontiers in molecular biosciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The Smc5/6 complex is a vital protector of eukaryotic genome stability, coordinating DNA repair, replication fork maintenance, recombination intermediate processing, and chromosome organization. Within this complex, the Nse5/6 heterodimer has recently emerged as a key factor influencing Smc5/6 dynamics, acting at the interface of structural control, enzymatic regulation, and chromatin recruitment. Structural studies from yeast to mammals show that Nse5/6 associate with the Smc5/6 head-neck region, restricting ATPase head engagement and stabilizing an inactive, chromatin-loading-ready state. Upon ATP binding and DNA interaction, conformational changes displace or reposition Nse5/6, facilitating Nse4-mediated head closure, DNA entrapment, and loop-modulating activity. Functional analyses across
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