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<p>The HSP90/R2TP quaternary chaperone assembles key cellular machines, including the three nuclear RNA polymerases and many non-coding RNPs. Here, we characterize the RNAs associated with R2TP and find that it binds many proteins co-translationally. Its co-translational interactome reveals potential clients and distinguishes clients bound only co-translationally, only post-translationally, or both. For subunits assembling together in the same complex and bound co-translationally by R2TP, only a marginal proportion of their mRNAs is co-localized and co-translated. Instead, HSP90 and R2TP induce the formation of polysome condensates accumulating these chaperones and specific client mRNAs, thus favoring co-translational interactions between them. During the assembly process, R2TP cycles between co- and post-translational steps and this is regulated by ATP: it binds co-translationally in absence of ATP and becomes released from post-translational assembly intermediates by ATP hydrolysis. This co-translational mechanism, named co-translational chaperone channeling (cha-cha), substitutes for the rarity of co-localized/co-translated mRNAs. In turn, chaperones have the remarkable ability to spatially organize the translational apparatus in the cytoplasm.</p>

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Co-translational determination of quaternary structures in chaperone factories

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年1月23日

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  • Manon Philippe,
  • Soha Salloum,
  • Floric Slimani,
  • Davide Normanno,
  • Isabelle Barbosa,
  • Héloïse Chassé,
  • Marie-Cécile Robert,
  • Serge Urbach,
  • Jacques Imbert,
  • Martial Séveno,
  • Simon George,
  • Hervé Le Hir,
  • Séverine Boulon,
  • Céline Verheggen,
  • Edouard Bertrand

摘要

The HSP90/R2TP quaternary chaperone assembles key cellular machines, including the three nuclear RNA polymerases and many non-coding RNPs. Here, we characterize the RNAs associated with R2TP and find that it binds many proteins co-translationally. Its co-translational interactome reveals potential clients and distinguishes clients bound only co-translationally, only post-translationally, or both. For subunits assembling together in the same complex and bound co-translationally by R2TP, only a marginal proportion of their mRNAs is co-localized and co-translated. Instead, HSP90 and R2TP induce the formation of polysome condensates accumulating these chaperones and specific client mRNAs, thus favoring co-translational interactions between them. During the assembly process, R2TP cycles between co- and post-translational steps and this is regulated by ATP: it binds co-translationally in absence of ATP and becomes released from post-translational assembly intermediates by ATP hydrolysis. This co-translational mechanism, named co-translational chaperone channeling (cha-cha), substitutes for the rarity of co-localized/co-translated mRNAs. In turn, chaperones have the remarkable ability to spatially organize the translational apparatus in the cytoplasm.