RAPP-containing arrest peptides induce translational stalling by short circuiting the ribosomal peptidyltransferase activity

Martino Morici, Sara Gabrielli, Keigo Fujiwara, Helge Paternoga, Bertrand Beckert, Lars V. Bock, Shinobu Chiba () and Daniel N. Wilson ()
Additional contact information
Martino Morici: University of Hamburg
Sara Gabrielli: Max Planck Institute for Multidisciplinary Sciences
Keigo Fujiwara: Kyoto Sangyo University
Helge Paternoga: University of Hamburg
Bertrand Beckert: University of Hamburg
Lars V. Bock: Max Planck Institute for Multidisciplinary Sciences
Shinobu Chiba: Kyoto Sangyo University
Daniel N. Wilson: University of Hamburg

Nature Communications, 2024, vol. 15, issue 1, 1-16

Abstract: Abstract Arrest peptides containing RAPP (ArgAlaProPro) motifs have been discovered in both Gram-positive and Gram-negative bacteria, where they are thought to regulate expression of important protein localization machinery components. Here we determine cryo-EM structures of ribosomes stalled on RAPP arrest motifs in both Bacillus subtilis and Escherichia coli. Together with molecular dynamics simulations, our structures reveal that the RAPP motifs allow full accommodation of the A-site tRNA, but prevent the subsequent peptide bond from forming. Our data support a model where the RAP in the P-site interacts and stabilizes a single hydrogen atom on the Pro-tRNA in the A-site, thereby preventing an optimal geometry for the nucleophilic attack required for peptide bond formation to occur. This mechanism to short circuit the ribosomal peptidyltransferase activity is likely to operate for the majority of other RAPP-like arrest peptides found across diverse bacterial phylogenies.

Date: 2024
References: View references in EconPapers View complete reference list from CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/s41467-024-46761-3 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-46761-3

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-024-46761-3

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().