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Instruments / Technical Area	Publication Details	Published	Actions
Krios I-Titan Krios I at Diamond	eIF6 rebinding dynamically couples ribosome maturation and translation Pekka Jaako , Alexandre Faille , Shengjiang Tan , Chi C. Wong , Norberto Escudero-Urquijo , Pablo Castro-Hartmann , Penny Wright , Christine Hilcenko , David J. Adams , Alan J. Warren Nature Communications 13 DOI: 10.1038/s41467-022-29214-7 Diamond Proposal Number(s): [22238] Open Access Show Abstract ▼ Abstract: Protein synthesis is a cyclical process consisting of translation initiation, elongation, termination and ribosome recycling. The release factors SBDS and EFL1—both mutated in the leukemia predisposition disorder Shwachman-Diamond syndrome — license entry of nascent 60S ribosomal subunits into active translation by evicting the anti-association factor eIF6 from the 60S intersubunit face. We find that in mammalian cells, eIF6 holds all free cytoplasmic 60S subunits in a translationally inactive state and that SBDS and EFL1 are the minimal components required to recycle these 60S subunits back into additional rounds of translation by evicting eIF6. Increasing the dose of eIF6 in mice in vivo impairs terminal erythropoiesis by sequestering post-termination 60S subunits in the cytoplasm, disrupting subunit joining and attenuating global protein synthesis. These data reveal that ribosome maturation and recycling are dynamically coupled by a mechanism that is disrupted in an inherited leukemia predisposition disorder.	Mar 2022
Krios II-Titan Krios II at Diamond	Mechanism of completion of peptidyltransferase centre assembly in eukaryotes Vasileios Kargas , Pablo Castro-Hartmann , Norberto Escudero-Urquijo , Kyle Dent , Christine Hilcenko , Carolin Sailer , Gertrude Zisser , Maria J. Marques-Carvalho , Simone Pellegrino , Leszek Wawiórka , Stefan M. V. Freund , Jane L. Wagstaff , Antonina Andreeva , Alexandre Faille , Edwin Chen , Florian Stengel , Helmut Bergler , Alan John Warren Elife 8 DOI: 10.7554/eLife.44904 Diamond Proposal Number(s): [14359, 15368, 16940, 17057, 18078, 18328] Show Abstract ▼ Abstract: 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.	May 2019

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