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Author Correction: A multipoint guidance mechanism for β-barrel folding on the SAM complex
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A multipoint guidance mechanism for β-barrel folding on the SAM complex
Mitochondrial β-barrel proteins are essential for the transport of metabolites, ions and proteins. The sorting and assembly machinery (SAM) mediates their folding and membrane insertion. We report the cryo-ele...
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Article
Quality control of the mitochondrial proteome
Mitochondria contain about 1,000–1,500 proteins that fulfil multiple functions. Mitochondrial proteins originate from two genomes: mitochondrial and nuclear. Hence, proper mitochondrial function requires synch...
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Article
RQT complex dissociates ribosomes collided on endogenous RQC substrate SDD1
Ribosome-associated quality control (RQC) represents a rescue pathway in eukaryotic cells that is triggered upon translational stalling. Collided ribosomes are recognized for subsequent dissociation followed b...
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Article
Structure of the Bcs1 AAA-ATPase suggests an airlock-like translocation mechanism for folded proteins
Some proteins require completion of folding before translocation across a membrane into another cellular compartment. Yet the permeability barrier of the membrane should not be compromised and mechanisms have ...
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Article
Structure of the 80S ribosome–Xrn1 nuclease complex
Messenger RNA (mRNA) homeostasis represents an essential part of gene expression, in which the generation of mRNA by RNA polymerase is counter-balanced by its degradation by nucleases. The conserved 5′-to-3′ e...
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Ribosome–NatA architecture reveals that rRNA expansion segments coordinate N-terminal acetylation
The majority of eukaryotic proteins are N-terminally α-acetylated by N-terminal acetyltransferases (NATs). Acetylation usually occurs co-translationally and defects have severe consequences. Nevertheless, it i...
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Open AccessThe novel TRAIL-receptor agonist APG350 exerts superior therapeutic activity in pancreatic cancer cells
Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) has raised attention as a novel anticancer therapeutic as it induces apoptosis preferentially in tumor cells. However, first-generation TRAIL-rec...
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Structure of the 40S–ABCE1 post-splitting complex in ribosome recycling and translation initiation
Cryo-EM structures of the yeast 40S in complex with ribosome-splitting protein ABCE1, along with functional analyses, reveal that the FeS cluster domain undergoes a 150° rotation to dissociate ribosomal subunits.
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Mitochondriale Systeme für den Import von Proteinen
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Structure of the no-go mRNA decay complex Dom34–Hbs1 bound to a stalled 80S ribosome
Messenger RNAs (mRNAs) that induce stalling during translation are degraded by a quality control mechanism known as no-go decay (NGD). The aberrant mRNAs are recognized by two factors, Dom34 and Hbs1. Using cr...
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Cryo-EM structure of the ribosome–SecYE complex in the membrane environment
A cryo-EM structure of the bacterial ribosome–SecYEG complex in a so-called Nanodisc allows for the molecular interpretation of the SecYEG complex in its natural lipid bilayer environment. Molecular dynamics s...
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Common ground for protein translocation: access control for mitochondria and chloroplasts
The vast majority of mitochondrial and chloroplast proteins are cytosolically synthesized and have to be translocated into the organelle.
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ERj1p uses a universal ribosomal adaptor site to coordinate the 80S ribosome at the membrane
Ribosomes translating secretory and membrane proteins are targeted to the endoplasmic reticulum membrane and attach to the protein-conducting channel and ribosome-associated membrane proteins (RAMPs). Recently...
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Localization and dynamic behavior of ribosomal protein L30e
The ribosomal protein L30e is an indispensable component of the eukaryotic 80S ribosome, where it is part of the large (60S) ribosomal subunit. Here, we determined the localization of L30e in the cryo-EM map o...