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. 2022 Jun 9;19(1):781–810. doi: 10.1080/15476286.2022.2079890

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© 2022 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.

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

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Figure 4. — Cryo-EM structures of helicases Dhr1 and Has1 bound to their pre-ribosomal substrate particles. (A) Dhr1 (red) bound to 90S (left panel, PDB: 6ZQD) or pre-40S (right panel, PDB: 6ZQG) particles. The assembly factors Utp14 (cyan) and Pno1 (blue) in proximity to the Dhr1 C-terminus, as well as the U3 snoRNA (black) and 25S rRNA H1 (Orange, right panel) base-pairing with U3 box A are depicted. (B) Has1 (red) binds to pre-60S intermediates (PDB: 5Z3G) on top of the ITS2-containing foot structure close to Nsa3. The two RecA-like domains interact with H16 (purple) of 25S rRNA domain I. The Has1 25S rRNA crosslink site at H21/H22 (Orange) and further proximal assembly factors and -r-proteins are indicated.