Article
|
Open Access
Featured
-
-
Article
| Open AccessTranslation selectively destroys non-functional transcription complexes
Translation actively dislodges stalled transcription elongation complexes (ECs) from damaged DNA, which enables lesion repair and restoration of transcription activity, and coupled ribosomes discriminate between active ECs and stalled ECs, ensuring destruction of only the latter.
- Jason Woodgate
- , Hamed Mosaei
- & Nikolay Zenkin
-
Article
| Open AccessStructural basis of ribosomal 30S subunit degradation by RNase R
Cryo-electron microscopy structures of intermediates formed during the degradation of the 30S ribosomal unit shed light on how the 3′ to 5′ exonuclease ribonuclease R controls the ribosomal degradation process.
- Lyudmila Dimitrova-Paternoga
- , Sergo Kasvandik
- & Helge Paternoga
-
Article |
mRNA reading frame maintenance during eukaryotic ribosome translocation
The accuracy of eukaryotic ribosome translocation relies on eukaryote-specific elements of the 80S ribosome, elongation factor 2 and transfer RNAs, all of which contribute to the maintenance of the messenger RNA reading frame.
- Nemanja Milicevic
- , Lasse Jenner
- & Gulnara Yusupova
-
Article |
Nuclear export of pre-60S particles through the nuclear pore complex
We report the cryo-electron microscopy structure of native pre-60S particles trapped in the channel of the yeast nuclear pore complex, suggesting a translocation model for the export of pre-60S particles through the complex.
- Zongqiang Li
- , Shuaijiabin Chen
- & Sen-Fang Sui
-
Article
| Open AccessmRNA decoding in human is kinetically and structurally distinct from bacteria
The reaction coordinate of aminoacyl-tRNA movement is altered on the human ribosome and the process is an order of magnitude slower compared with bacteria due to eukaryote-specific structural elements in the human ribosome and in the elongation factor eEF1A.
- Mikael Holm
- , S. Kundhavai Natchiar
- & Scott C. Blanchard
-
Article |
A molecular network of conserved factors keeps ribosomes dormant in the egg
Mass spectrometry and structural studies demonstrate the specific changes in protein composition that accompany the transition of ribosomes in zebrafish and Xenopus eggs from a dormant to an active state during early embryogenesis.
- Friederike Leesch
- , Laura Lorenzo-Orts
- & Andrea Pauli
-
Article |
A male germ-cell-specific ribosome controls male fertility
RibosomeST—a ribosome with a specialized nascent polypeptide exit tunnel—cotranslationally regulates the folding of a subset of male germ-cell-specific proteins that are essential for the formation of sperm.
- Huiling Li
- , Yangao Huo
- & Jiahao Sha
-
Article
| Open AccessVisualizing translation dynamics at atomic detail inside a bacterial cell
Cryo-electron tomography is used to reveal the structural dynamics and functional diversity of translating ribosomes in Mycoplasma pneumoniae, providing insight into the translation elongation cycle inside cells and how it is reshaped by antibiotics.
- Liang Xue
- , Swantje Lenz
- & Julia Mahamid
-
Article |
eIF5B and eIF1A reorient initiator tRNA to allow ribosomal subunit joining
Single-molecule spectroscopy and structural studies were used to examine the dynamics of association of eIF1A and eIF5B with the human translation initiation complex and their role in presenting tRNA to the complex to initiate translation.
- Christopher P. Lapointe
- , Rosslyn Grosely
- & Joseph D. Puglisi
-
Article
| Open AccessMechanism of mitoribosomal small subunit biogenesis and preinitiation
Structural analysis of several small mitoribosomal subunit intermediates reveals a sequential mechanism of biogenesis, and how assembly links to initiation to form active mitoribosomes.
- Yuzuru Itoh
- , Anas Khawaja
- & Alexey Amunts
-
Matters Arising |
Evaluating ribosomal frameshifting in CCR5 mRNA decoding
- Yousuf A. Khan
- , Gary Loughran
- & John F. Atkins
-
Article |
Ribosome collisions induce mRNA cleavage and ribosome rescue in bacteria
In bacteria, a newly identified endonuclease activated by ribosome collisions truncates mRNA to trigger rescue of stalled ribosomes.
- Kazuki Saito
- , Hanna Kratzat
- & Allen R. Buskirk
-
Article |
Bacterial ribosome collision sensing by a MutS DNA repair ATPase paralogue
Bacterial MutS2, a paralogue of the DNA mismatch-repair protein MutS, is found to bind collided ribosomes and function in translational quality control.
- Federico Cerullo
- , Sebastian Filbeck
- & Claudio A. P. Joazeiro
-
Article
| Open AccessAccuracy mechanism of eukaryotic ribosome translocation
Structural analysis of the Saccharomyces cerevisiae 80S ribosome trapped in an intermediate translocation state shows stabilization of codon–anticodon interactions by eukaryote-specific elements of the 80S ribosome, eEF2 and tRNA and demonstrates a major role for eEF2 in maintaining the directionality of translocation.
- Muminjon Djumagulov
- , Natalia Demeshkina
- & Gulnara Yusupova
-
Article |
Cotranslational prolyl hydroxylation is essential for flavivirus biogenesis
A proteomics-based strategy is used to examine how three different RNA viruses (polio, Zika and dengue) remodel translation in the host to recruit host machineries necessary for the production of viral proteins.
- Ranen Aviner
- , Kathy H. Li
- & Raul Andino
-
Article
| Open AccessStructural basis of early translocation events on the ribosome
Cryo-electron microscopy and single-molecule fluorescence methods are used to elucidate the mechanism of early translocation events on the bacterial ribosome.
- Emily J. Rundlet
- , Mikael Holm
- & Scott C. Blanchard
-
Article |
Structural basis for the final steps of human 40S ribosome maturation
Studies of five cryo-electron microscopy structures reveal the composition and conformational progression in the final maturation events of human 40S ribosomal subunit assembly.
- Michael Ameismeier
- , Ivo Zemp
- & Roland Beckmann
-
Article |
The coding capacity of SARS-CoV-2
A high-resolution map of coding regions in the SARS-CoV-2 genome enables the identification of 23 unannotated open reading frames and quantification of the expression of canonical viral open reading frames.
- Yaara Finkel
- , Orel Mizrahi
- & Noam Stern-Ginossar
-
Article |
Functionally uncoupled transcription–translation in Bacillus subtilis
In Bacillus subtilis, unlike in Escherichia coli, transcription and translation of genes are not tightly coupled, and pioneering ribosomes lag substantially behind RNA polymerases.
- Grace E. Johnson
- , Jean-Benoît Lalanne
- & Gene-Wei Li
-
Article |
Cryo-EM of elongating ribosome with EF-Tu•GTP elucidates tRNA proofreading
Time-resolved cryogenic electron microscopy structures of a ribosome during the delivery of aminoacyl-tRNA by EF-Tu•GTP capture 33 ribosomal states, enabling visualization of the initial selection, proofreading and peptidyl transfer stages.
- Anna B. Loveland
- , Gabriel Demo
- & Andrei A. Korostelev
-
Article |
DNA-PKcs has KU-dependent function in rRNA processing and haematopoiesis
The catalytic subunit of DNA-PK autophosphorylates and contributes to ribosome biogenesis and haematopoiesis by binding to the U3 small nucleolar RNA.
- Zhengping Shao
- , Ryan A. Flynn
- & Eliezer Calo
-
Letter |
eIF5B gates the transition from translation initiation to elongation
Single-molecule dynamics reveal that the GTPase activity of eukaryotic initiation factor eIF5B serves as a kinetic checkpoint for the transition from translation initiation to elongation.
- Jinfan Wang
- , Alex G. Johnson
- & Joseph D. Puglisi
-
Letter |
Late steps in bacterial translation initiation visualized using time-resolved cryo-EM
A time-resolved cryo-electron microscopy approach is used to visualize, at near-atomic resolution and on a sub-second timescale, short-lived intermediate states of a fundamental biomolecular reaction.
- Sandip Kaledhonkar
- , Ziao Fu
- & Joachim Frank
-
Letter |
Controlling orthogonal ribosome subunit interactions enables evolution of new function
Orthogonal ribosomes are engineered in which the two subunits are stapled together in a way that limits association with endogenous subunits in cells, enabling the evolution of new functionality in the orthogonal ribosome.
- Wolfgang H. Schmied
- , Zakir Tnimov
- & Jason W. Chin
-
Letter |
Cotranslational assembly of protein complexes in eukaryotes revealed by ribosome profiling
Cotranslational assembly is a prevalent mechanism for the formation of oligomeric complexes in Saccharomyces cerevisiae, with one subunit serving as scaffold for the translation of partner subunits.
- Ayala Shiber
- , Kristina Döring
- & Bernd Bukau
-
Letter |
Unique features of mammalian mitochondrial translation initiation revealed by cryo-EM
A cryo-electron microscopy structure of the mammalian mitochondrial translation initiation complex reveals unique features that are necessary to initiate mitochondrial translation and highlights a possible membrane-targeting peptide.
- Eva Kummer
- , Marc Leibundgut
- & Nenad Ban
-
Article |
Visualizing late states of human 40S ribosomal subunit maturation
Cryo-EM structures of late intermediates in the assembly of human 40S ribosomal subunits help to define the principles by which immature rRNA conformations and ribosomal biogenesis factors shape the 40S maturation process.
- Michael Ameismeier
- , Jingdong Cheng
- & Roland Beckmann
-
Letter |
An evolutionarily conserved ribosome-rescue pathway maintains epidermal homeostasis
Loss of the ribosome-rescue factor Pelo in a subset of mouse epidermal stem cells results in hyperproliferation and altered differentiation of these cells.
- Kifayathullah Liakath-Ali
- , Eric W. Mills
- & Fiona M. Watt
-
Letter |
Vms1 and ANKZF1 peptidyl-tRNA hydrolases release nascent chains from stalled ribosomes
The Cdc48 adaptor Vms1 is a peptidyl-tRNA hydrolase that cooperates with the ribosome quality control complex to catalyse the removal of nascent polypeptides from stalled ribosomes.
- Rati Verma
- , Kurt M. Reichermeier
- & Raymond J. Deshaies
-
Article |
Visualization of chemical modifications in the human 80S ribosome structure
A high-resolution structure of the human ribosome determined by cryo-electron microscopy visualizes numerous RNA modifications that are concentrated at functional sites with an extended shell, and suggests the possibility of designing more specific ribosome-targeting drugs.
- S. Kundhavai Natchiar
- , Alexander G. Myasnikov
- & Bruno P. Klaholz
-
Analysis |
Ribosomes are optimized for autocatalytic production
The large number of small, similarly sized proteins and the small number of heavy RNA molecules that make up a ribosome reduce the time required for reproduction.
- Shlomi Reuveni
- , Måns Ehrenberg
- & Johan Paulsson
-
Letter |
Trans-kingdom mimicry underlies ribosome customization by a poxvirus kinase
The poxvirus vaccinia virus phosphorylates serine/threonine residues in the human small ribosomal subunit RACK1, converting it to a plant-like state to favour translation of poxvirus mRNAs
- Sujata Jha
- , Madeline G. Rollins
- & Derek Walsh
-
Article |
Ensemble cryo-EM elucidates the mechanism of translation fidelity
Structural ensembles of the 70S ribosome bound to cognate or near-cognate charged tRNAs in complex with EF-Tu illustrate the crucial role of the nucleotide G530 in decoding of mRNA, and demonstrate that translational fidelity results from direct control of GTPase by the decoding centre.
- Anna B. Loveland
- , Gabriel Demo
- & Andrei A. Korostelev
-
Letter |
Structural basis of co-translational quality control by ArfA and RF2 bound to ribosome
The structure of the bacterial ribosome in complex with the ArfA and the release factor RF2 shows how ArfA recruits RF2 to terminate translation of messenger RNAs that lack a stop codon in the ribosome.
- Fuxing Zeng
- , Yanbo Chen
- & Hong Jin
-
Letter |
Mechanistic insights into the alternative translation termination by ArfA and RF2
The structure of the bacterial 70S ribosome in complex with ArfA, the release factor RF2, a short non-stop mRNA and a cognate P-site tRNA is presented, revealing how ArfA and RF2 facilitate alternative translation termination of the non-stop ribosomal complex using a stop-codon surrogate mechanism.
- Chengying Ma
- , Daisuke Kurita
- & Ning Gao
-
Letter |
Structural basis for ArfA–RF2-mediated translation termination on mRNAs lacking stop codons
The structure of the bacterial ribosome stalled on a truncated mRNA in complex with ArfA and the release factor RF2 is presented, revealing how ArfA recruits RF2 to the ribosome and induces conformational changes within RF2 to enable translation termination in the absence of a stop codon.
- Paul Huter
- , Claudia Müller
- & Daniel N. Wilson
-
Article |
The pathway to GTPase activation of elongation factor SelB on the ribosome
The structures of several states on the pathway of SelB-mediated delivery of selenocysteine-specific tRNA to the ribosome in Escherichia coli reveal the mechanism of UGA stop codon recoding to selenocysteine and show how codon recognition triggers activation of translational GTPases.
- Niels Fischer
- , Piotr Neumann
- & Holger Stark
-
Letter |
Cotranslational signal-independent SRP preloading during membrane targeting
The signal recognition particle (SRP) preferentially binds peptides destined for secretion before peptide-targeting signals are translated through recognition of elements in their mRNA, including non-coding sequences.
- Justin W. Chartron
- , Katherine C. L. Hunt
- & Judith Frydman
-
Letter |
Global profiling of SRP interaction with nascent polypeptides
Here, the selection of substrates by the protein–RNA complex known as the signal recognition particle (SRP) is investigated in the bacterium Escherichia coli, revealing that the SRP has a strong preference for hydrophobic transmembrane domains of inner membrane proteins.
- Daniela Schibich
- , Felix Gloge
- & Günter Kramer
-
Letter |
Dynamics of ribosome scanning and recycling revealed by translation complex profiling
A translation complex sequencing approach has been developed enabling intermediates of all mRNA-associated processes of translation to be isolated and localized across the transcriptome; the results support longstanding models of initiation and termination and offer new mechanistic insights.
- Stuart K. Archer
- , Nikolay E. Shirokikh
- & Thomas Preiss
-
Letter |
Translation readthrough mitigation
Translation termination sequences are occasionally bypassed by the ribosome and the resulting proteins can be detrimental to the cell; here it is shown that cells can prevent such proteins from accumulating through peptides that are encoded within the 3' UTR of genes in both humans and C. elegans.
- Joshua A. Arribere
- , Elif S. Cenik
- & Andrew Z. Fire
-
Letter |
Diverse roles of assembly factors revealed by structures of late nuclear pre-60S ribosomes
The cryo-electron microscopy structures of yeast nucleoplasmic pre-60S ribosomal particles give insight into the function of multiple assembly factors in ribosome biogenesis.
- Shan Wu
- , Beril Tutuncuoglu
- & Ning Gao
-
Article |
Synchronized mitochondrial and cytosolic translation programs
The genes encoding the subunits of oxidative phosphorylation complexes are split between the nuclear and mitochondrial genomes, but their translation is synchronized by signalling from the cytosol to the mitochondria.
- Mary T. Couvillion
- , Iliana C. Soto
- & L. Stirling Churchman
-
Letter |
Ribosome-dependent activation of stringent control
The structure of a bacterial ribosome–RelA complex reveals that RelA, a protein recruited to the ribosome in the case of scarce amino acids, binds in a different location to translation factors, and that this binding event suppresses auto-inhibition to activate synthesis of the (p)ppGpp secondary messenger, thus initiating stringent control.
- Alan Brown
- , Israel S. Fernández
- & V. Ramakrishnan
-
Article |
Structure of mammalian eIF3 in the context of the 43S preinitiation complex
The cryo-electron microscopy structure of the eukaryotic initiation factor 3 (eIF3) within the larger 43S complex is determined; the improved resolution enables visualization of the secondary structures of the subunits, as well as the contacts between eIF3 and both eIF2 and DHX29.
- Amedee des Georges
- , Vidya Dhote
- & Yaser Hashem
-
Letter |
Structural basis for stop codon recognition in eukaryotes
All eukaryotes utilize a single termination factor, eRF1, to halt translation when the ribosome encounters one of three possible stop codons; here electron cryo-microscopy structures of ribosome–eRF1 complexes in the process of recognizing each stop codon reveal how stop codons are discriminated from sense codons.
- Alan Brown
- , Sichen Shao
- & V. Ramakrishnan
-
Letter |
Protein synthesis by ribosomes with tethered subunits
A ribosome with tethered subunits, ‘Ribo-T’, is engineered by making a hybrid RNA composed of ribosomal RNA of large and small subunits; Ribo-T can support cell growth in vivo in the absence of wild-type ribosomes, and is used to establish a fully orthogonal ribosome–mRNA system.
- Cédric Orelle
- , Erik D. Carlson
- & Alexander S. Mankin
-
Article |
Structure of the human 80S ribosome
The structure of the human ribosome at high resolution has been solved; by combining single-particle cryo-EM and atomic model building, local resolution of 2.9 Å was achieved within the most stable areas of the structure.
- Heena Khatter
- , Alexander G. Myasnikov
- & Bruno P. Klaholz
-
Letter |
Structure of the E. coli ribosome–EF-Tu complex at <3 Å resolution by Cs-corrected cryo-EM
A single particle cryo-EM structure of the 70S ribosome in complex with the elongation factor Tu breaks the 3 Å resolution barrier of the technique and locally exceeds the resolution of previous crystallographic studies, revealing all modifications in rRNA and explaining their roles in ribosome function and antibiotic binding.
- Niels Fischer
- , Piotr Neumann
- & Holger Stark