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 J. Warren +17 more
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TLDR
The mechanism of peptidyltransferase centre (PTC) completion is presented that explains how integration of the last ribosomal proteins is coupled to release of the nuclear export adaptor Nmd3 and reveals how the central functional site of the ribosome is sculpted.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.read more
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Mechanisms and regulation of protein synthesis in mitochondria
Eva Kummer,Nenad Ban +1 more
TL;DR: In this paper, the authors review fundamental insights that have been made into the biogenesis, architecture and mechanisms of the mitochondrial translation apparatus in the past years owing to the emergence of numerous near-atomic structures and a considerable amount of biochemical work.
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Stress-Induced Translation Inhibition through Rapid Displacement of Scanning Initiation Factors.
Stefan Bresson,Vadim Shchepachev,Christos Spanos,Tomasz W. Turowski,Juri Rappsilber,Juri Rappsilber,David Tollervey +6 more
TL;DR: Mechanisms underlying translational control of gene expression during stress are revealed, particularly for translation-related factors, mediated by Xrn1.
Journal ArticleDOI
Construction of the Central Protuberance and L1 Stalk during 60S Subunit Biogenesis.
Lukas Kater,Valentin Mitterer,Matthias Thoms,Matthias Thoms,Jingdong Cheng,Otto Berninghausen,Roland Beckmann,Ed Hurt +7 more
TL;DR: Two nuclear pre-60S intermediates were discovered that represent previously unknown states after Rea1-mediated removal of the Ytm1-Erb1 complex and reveal how the L1 stalk develops from a pre-mature nucleolar to a mature-like nucleoplasmic state.
Journal ArticleDOI
The GTPase Nog1 co-ordinates the assembly, maturation and quality control of distant ribosomal functional centers.
Purnima Klingauf-Nerurkar,Ludovic C Gillet,Daniela Portugal-Calisto,Michaela Oborská-Oplová,Michaela Oborská-Oplová,Martin Jäger,Olga T. Schubert,Agnese Pisano,Cohue Peña,Sanjana Rao,Martin Altvater,Yiming Chang,Ruedi Aebersold,Ruedi Aebersold,Vikram Govind Panse +14 more
TL;DR: It is revealed that sequential ATPase and GTPase activities license release factors Rei1 and Yvh1 to trigger Arx1 and Mrt4 removal and Nog1 co-ordinates the assembly, maturation and quality control of distant functional centers during ribosome formation.
Journal ArticleDOI
Structural snapshots of human pre-60S ribosomal particles before and after nuclear export.
Xiaomeng Liang,Xiaomeng Liang,Mei-Qing Zuo,Mei-Qing Zuo,Yunyang Zhang,Ningning Li,Chengying Ma,Meng-Qiu Dong,Ning Gao +8 more
TL;DR: A structural analysis of a collection of human pre- 60S structures sampled through a nuclear export adaptor NMD3, representing structural snapshots of pre-60S particles immediately before and after passing through nuclear pore complex facilitates the understanding of the global conservation of ribosome assembly in eukaryotes and species-specific features of human assembly factors.
References
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