Journal
ELIFE
Volume 8, Issue -, Pages -Publisher
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.44904
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Funding
- Medical Research Council [MC_U105161083]
- Bloodwise [12048]
- Wellcome [108466/Z/15/Z]
- Deutsche Forschungsgemeinschaft Emmy Noether Programme [STE 2517/1-1]
- Deutsche Forschungsgemeinschaft Collaborative Research Center 969
- Fonds zur Forderung der Wissenschaftlichen Forschung FWF Grants [P26136, P29451]
- Wellcome Trust [108466/Z/15/Z] Funding Source: Wellcome Trust
- MRC [MC_UP_1201/14, MR/L003368/1, MC_U105184326, MC_U105161083] Funding Source: UKRI
- Austrian Science Fund (FWF) [P26136, P29451] Funding Source: Austrian Science Fund (FWF)
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During their final maturation in the cytoplasm, pre-60S ribosomal particles are converted to translation-competent large ribosomal subunits. Here, we present the mechanism of peptidyltransferase centre (PTC) completion that explains how integration of the last ribosomal proteins is coupled to release of the nuclear export adaptor Nmd3. Single-particle cryo-EM reveals that eL40 recruitment stabilises helix 89 to form the uL16 binding site. The loading of uL16 unhooks helix 38 from Nmd3 to adopt its mature conformation. In turn, partial retraction of the L1 stalk is coupled to a conformational switch in Nmd3 that allows the uL16 P-site loop to fully accommodate into the PTC where it competes with Nmd3 for an overlapping binding site (base A2971). Our data reveal how the central functional site of the ribosome is sculpted and suggest how the formation of translation-competent 60S subunits is disrupted in leukaemia-associated ribosomopathies.
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