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. 2023 Apr 10;30(5):594–599. doi: 10.1038/s41594-023-00947-3

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© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Extended Data Fig. 8 — (a) A top view down the central cavity of the Noc1-Noc2 heterodimer encapsulating helix 2 of the large subunit rRNA. The most conserved residues of the heterodimer are depicted in spheres, with sequence conservation colored from coral (100% conserved) to white (0% conserved) for Noc1, and maroon (100% conserved) to white (0% conserved) for Noc2. Conservation was calculated by the ConSurf webserver⁴⁰, with sequence alignments generated by Clustal Omega⁴¹ from 12 model organisms. (b) The Noc1-Noc2 interface highlights clusters of conserved residues that allow for a tight interaction between the two proteins, with conserved residues depicted in sticks. (c) The Noc1-RNA interface reveals a set of conserved residues that line the central channel occupied by the RNA of helix 2, depicted in sticks.