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. 2022 Dec 30;51(1):253–270. doi: 10.1093/nar/gkac1172

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© The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 8. — A model for the role of Cue2 in two modes of NGD. A model for Cue2 recognition of the substrates of two modes of NGD induced by the rare codon staller. A model for NGD^RQC− (left): Hel2 forms K63-linked polyubiquitin chains on eS7 (shown in blue circles) of the colliding ribosome in the trisome formed on the SDD1 mRNA. Cue2 binds to the K63-linked polyubiquitin chains on eS7 with two CUE domains, CUE-D1 and CUE-D2. The Cue2 bound to the stalled ribosome cleaves the mRNA upstream of the colliding ribosome 2 (collided 2). A model for NGD^RQC+ (right): Hel2 ubiquitinates uS10 on the leading ribosome and the RQT complex recognizes the polyubiquitinated uS10 (shown in red circles). The Slh1 helicase subunit of RQT applies a pulling force on the mRNA, leading to the dissociation of the leading ribosome into subunits. The collided ribosome 1 (collided 1) functions as a ram or giant wedge, but mRNA is partially released. After pulling of mRNA by the RQT complex, Cue2 cleaves mRNA partially released from the colliding ribosome 1.