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- W3044338510 abstract "Significance The dynein-like AAA motor Mdn1 drives ribosome biogenesis by using ATP-fueled motions to dislodge assembly factor proteins from 60S precursor particles. It is not known how this unusually large (>500 kDa) mechanoenzyme coordinates the activities of its C-terminal MIDAS domain, which binds specific preribosomal proteins, with the ATPase cycle in its N-terminal AAA ring. Here, we show that the linking domains, which include a >500-amino acid disordered region, regulate an intramolecular binding interaction between the AAA and MIDAS domains. Surprisingly, the linking domains down-regulate MIDAS-AAA binding despite tethering these two domains together. This study provides insights into the regulation of Mdn1 function and into the design principles of large, multidomain mechanoenzymes." @default.
- W3044338510 created "2020-07-29" @default.
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- W3044338510 date "2020-07-21" @default.
- W3044338510 modified "2023-10-16" @default.
- W3044338510 title "Long-range intramolecular allostery and regulation in the dynein-like AAA protein Mdn1" @default.
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- W3044338510 doi "https://doi.org/10.1073/pnas.2002792117" @default.
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