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Tightly-orchestrated rearrangements govern catalytic center assembly of the ribosome.

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TLDR
In this paper, the structure of six intermediates in late nuclear and cytoplasmic maturation of the large subunit of the ribosome was determined, revealing a tightly-choreographed sequence of protein and RNA rearrangements controlling the insertion of Rpl10.
Abstract
The catalytic activity of the ribosome is mediated by RNA, yet proteins are essential for the function of the peptidyl transferase center (PTC). In eukaryotes, final assembly of the PTC occurs in the cytoplasm by insertion of the ribosomal protein Rpl10 (uL16). We determine structures of six intermediates in late nuclear and cytoplasmic maturation of the large subunit that reveal a tightly-choreographed sequence of protein and RNA rearrangements controlling the insertion of Rpl10. We also determine the structure of the biogenesis factor Yvh1 and show how it promotes assembly of the P stalk, a critical element for recruitment of GTPases that drive translation. Together, our structures provide a blueprint for final assembly of a functional ribosome.

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Signal Transduction in Ribosome Biogenesis: A Recipe to Avoid Disaster.

TL;DR: Some of the well-studied pathways known to control ribosome biogenesis (PI3K-AKT-mTOR, RB-p53, MYC) are examined and how they may interact with some of the less well studied pathways (eIF2α kinase and RNA editing/splicing) in higher eukaryotes to regulate ribosomes biogenesis, assembly, and protein translation in a dynamic manner are examined.
Journal ArticleDOI

Mechanism of completion of peptidyltransferase centre assembly in eukaryotes.

TL;DR: 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.
Journal ArticleDOI

Construction of the Central Protuberance and L1 Stalk during 60S Subunit Biogenesis.

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

Systematic Review of Plant Ribosome Heterogeneity and Specialization.

TL;DR: A data analysis pipeline is proposed that infers the heterogeneity of ribosome complexes and deviations from canonical structural compositions linked to stress events and can be extrapolated and enhanced by combination with other high-throughput methodologies, such as proteomics.
Journal ArticleDOI

The GTPase Nog1 co-ordinates the assembly, maturation and quality control of distant ribosomal functional centers.

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.
References
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Journal ArticleDOI

UCSF Chimera--a visualization system for exploratory research and analysis.

TL;DR: Two unusual extensions are presented: Multiscale, which adds the ability to visualize large‐scale molecular assemblies such as viral coats, and Collaboratory, which allows researchers to share a Chimera session interactively despite being at separate locales.
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Features and development of Coot.

TL;DR: Coot is a molecular-graphics program designed to assist in the building of protein and other macromolecular models and the current state of development and available features are presented.
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MotionCor2: Anisotropic Correction of Beam-Induced Motion for Improved Cryo-Electron Microscopy

TL;DR: MotionCor2 software corrects for beam-induced sample motion, improving the resolution of cryo-EM reconstructions.
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RELION: implementation of a Bayesian approach to cryo-EM structure determination.

TL;DR: Developments that reduce the computational costs of the underlying maximum a posteriori (MAP) algorithm, as well as statistical considerations that yield new insights into the accuracy with which the relative orientations of individual particles may be determined are described.
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