Nature Search

Structural 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
ResearchOpen Access07 Feb 2024
Nature

Volume: 626, P: 1133-1140
Publisher Correction: RAPP-containing arrest peptides induce translational stalling by short circuiting the ribosomal peptidyltransferase activity

Martino Morici
Sara Gabrielli
Daniel N. Wilson
Amendments and CorrectionsOpen Access15 Apr 2024
Nature Communications

Volume: 15, P: 1
Publisher Correction: The SecM arrest peptide traps a pre-peptide bond formation state of the ribosome

Felix Gersteuer
Martino Morici
Daniel N. Wilson
Amendments and CorrectionsOpen Access16 Apr 2024
Nature Communications

Volume: 15, P: 1
Structural conservation of antibiotic interaction with ribosomes

Here the authors present the high-resolution structures of 17 antibiotics bound to Escherichia coli ribosomes, which may inform the development of new antibacterial agents. Their results unveil a conserved manner of antibiotic binding to the ribosome, including ordered water molecules.

Helge Paternoga
Caillan Crowe-McAuliffe
Daniel N. Wilson
ResearchOpen Access07 Aug 2023
Nature Structural & Molecular Biology

Volume: 30, P: 1380-1392
The translation inhibitors kasugamycin, edeine and GE81112 target distinct steps during 30S initiation complex formation

The antibiotics kasugamycin, edeine and GE81112, inhibit translation initiation. Here, the authors present cryo-electron microscopy structures of 30S initiation intermediate complexes with these drugs revealing their mechanism of action.

Haaris A. Safdari
Martino Morici
Daniel N. Wilson
ResearchOpen Access12 Mar 2025
Nature Communications

Volume: 16, P: 1-12
Paenilamicins are context-specific translocation inhibitors of protein synthesis

The paenilamicins are hybrid nonribosomal peptide–polyketide compounds that inhibit protein synthesis. Here the authors reveal that paenilamicins bind to a unique site on the ribosome, where they interfere with the translocation of mRNA and tRNAs during elongation.

Timm O. Koller
Max J. Berger
Daniel N. Wilson
ResearchOpen Access17 Oct 2024
Nature Chemical Biology

Volume: 20, P: 1691-1700
The SecM arrest peptide traps a pre-peptide bond formation state of the ribosome

Stalling of ribosomes by the nascent polypeptide chain is widely used to regulate gene expression. Here, Gersteuer et al determine cryo-EM structures of SecM-stalled ribosomes revealing the mechanism by which the SecM peptide arrests translation.

Felix Gersteuer
Martino Morici
Daniel N. Wilson
ResearchOpen Access19 Mar 2024
Nature Communications

Volume: 15, P: 1-16
RAPP-containing arrest peptides induce translational stalling by short circuiting the ribosomal peptidyltransferase activity

Translation of RAPP (Arg-AlaPro-Pro) motifs induces ribosome stalling. Here, structures of RAPP-stalled ribosomes reveal that RAPP motifs short circuit the ribosomal peptidyltransferase activity to induce stalling.

Martino Morici
Sara Gabrielli
Daniel N. Wilson
ResearchOpen Access19 Mar 2024
Nature Communications

Volume: 15, P: 1-16

Search

Filter By:

Search

Quick links