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. 2022 Nov 2;50(20):11924–11937. doi: 10.1093/nar/gkac961

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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 6. — RRP12 is the central coordinator for head formation. (A) The N and C termini of RRP12 coordinate CK1 and position it close to BYSL and LTV1. The active center of the kinase domain is indicated with a red star. (B) The N-terminal ARM repeat of RRP12 interacts with the 142–167 region of BYSL. (C) The middle region of the ARM repeat of RRP12 interacts with the 47–91 region of BYSL. (D) The N terminus of BYSL (residues 18–39) interacts with PNO1. (E) The region of amino acids 174–225 of SLX9 interacts with the C-terminal ARM repeats of RRP12. (F) The region of amino acids 101–130 of SLX9 binds to the CPK region on the 40S body. (G) Two regions of RRP12 (residues 1070–1080 and 1145–1157) interact with eS17. (H) The very C terminus of RRP12 pokes through the h28 region and interacts with BUD23. Center: A schematic representation of the architecture of RRP12; thumbnails indicate the overall position of the respective assembly factor.