ArticlebioRxiv : the preprint server for biology2026
Chaperones shape the conformational landscape of 26S-proteasome-base assembly for allosteric ATPase motor activation.
Article in bioRxiv : the preprint server for biology, 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
Protein homeostasis depends on the 26S proteasome, the most complex ATP-dependent protease in eukaryotic cells. The proteasome base subcomplex is responsible for mechanical substrate unfolding and translocation into an internal degradation chamber. It contains three non-ATPase subunits, Rpn1, Rpn2, and Rpn13, and a heterohexameric AAA+ motor with six distinct ATPases, Rpt1 - Rpt6. Correct base assembly requires four dedicated chaperones that initially form the Hsm3 module (Hsm3-Rpt1-Rpt2-Rpn1), the Rpn14/Nas6 module (Rpn14-Rpt6-Nas6-Rpt3-Rpn2-Rpn13), and the Nas2 module (Nas2-Rpt5-Rpt4). However, the mechanisms underlying module assembly and formation of the mature base remain unknown. Here, we
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