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. 2017 Jan 23;45(8):4853–4865. doi: 10.1093/nar/gkw1361

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© The Author(s) 2017. 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 (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 7. — rRNA and AF neighborhoods affected in the erb1Δ161–200 and erb1Δ201–245 mutants. (A) Images of preribosomes showing the rRNA structural elements contacted by Erb1. Helices h76 and h88 in domain V (red) of 25S rRNA contact the binding site of Erb1 and Nop53 (yellow spheres) in domain I of 25S rRNA (27,28,81). The 3΄-end of 5.8S rRNA base-pairs with the 5΄-end of 25S rRNA in domain I to form the ITS2 proximal stem, which is also in close proximity with helix h79 (ES31). The 5΄-portion of 5.8S rRNA lines the polypeptide exit tunnel. (B) Nop7 binds to domain III of 25S rRNA (ES26), the ITS2 proximal stem, and h71 in domain V of 25S rRNA (27,28). The AFs Nsa2, Nog2, and Rsa4, whose association with preribosomes is perturbed in erb1Δ161–200 and erb1Δ201–245 mutants, bind next to the peptidyl transferase center (PTC) in domain V. Nop53 binds domain V of 25S rRNA and ITS2 proximal stem, adjacent to Nop7. Only partial structures of Nop7 and Nop53 are resolved in cryo-EM structures of Nog2-purified preribosomes (PDB ID: 3JCT) (28).