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

J 2024

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

MORICI, Martino; Sara GABRIELLI; Keigo FUJIWARA; Helge PATERNOGA; Bertrand BECKERT et al.

Základní údaje

Originální název

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

Autoři

MORICI, Martino; Sara GABRIELLI; Keigo FUJIWARA; Helge PATERNOGA; Bertrand BECKERT; Lars V BOCK; Shinobu CHIBA a Daniel N WILSON

Vydání

Nature Communications, Berlin, Nature, 2024, 2041-1723

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10400 1.4 Chemical sciences

Stát vydavatele

Německo

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 15.700

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:90043/24:00139055

Organizační jednotka

CIISB

Klíčová slova anglicky

BEAM-INDUCED MOTION; BOND FORMATION; BAYESIAN-APPROACH; A-SITECHAIN; SECM; PARAMETERS; GUIDELINES; INSIGHTS; MONITOR

Štítky

CF CRYO, ne MU, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 14. 3. 2025 15:23, Mgr. Eva Dubská

Anotace

V originále

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.

Návaznosti

90127, velká výzkumná infrastruktura

Název: CIISB II

Citovat

MORICI, Martino; Sara GABRIELLI; Keigo FUJIWARA; Helge PATERNOGA; Bertrand BECKERT; Lars V BOCK; Shinobu CHIBA a Daniel N WILSON. RAPP-containing arrest peptides induce translational stalling by short circuiting the ribosomal peptidyltransferase activity. Nature Communications. Berlin: Nature, 2024, roč. 15, č. 1, s. 1-16. ISSN 2041-1723. Dostupné z: https://doi.org/10.1038/s41467-024-46761-3.

@article{2483866,
   author = {Morici, Martino and Gabrielli, Sara and Fujiwara, Keigo and Paternoga, Helge and Beckert, Bertrand and Bock, Lars V and Chiba, Shinobu and Wilson, Daniel N},
   article_location = {Berlin},
   article_number = {1},
   doi = {https://doi.org/10.1038/s41467-024-46761-3},
   keywords = {BEAM-INDUCED MOTION; BOND FORMATION; BAYESIAN-APPROACH; A-SITECHAIN; SECM; PARAMETERS; GUIDELINES; INSIGHTS; MONITOR},
   language = {eng},
   issn = {2041-1723},
   journal = {Nature Communications},
   title = {RAPP-containing arrest peptides induce translational stalling by short circuiting the ribosomal peptidyltransferase activity},
   url = {https://www.nature.com/articles/s41467-024-46761-3},
   volume = {15},
   year = {2024}
}

TY  - JOUR
ID  - 2483866
AU  - Morici, Martino - Gabrielli, Sara - Fujiwara, Keigo - Paternoga, Helge - Beckert, Bertrand - Bock, Lars V - Chiba, Shinobu - Wilson, Daniel N
PY  - 2024
TI  - RAPP-containing arrest peptides induce translational stalling by short circuiting the ribosomal peptidyltransferase activity
JF  - Nature Communications
VL  - 15
IS  - 1
SP  - 1-16
EP  - 1-16
PB  - Nature
SN  - 20411723
KW  - BEAM-INDUCED MOTION
KW  - BOND FORMATION
KW  - BAYESIAN-APPROACH
KW  - A-SITECHAIN
KW  - SECM
KW  - PARAMETERS
KW  - GUIDELINES
KW  - INSIGHTS
KW  - MONITOR
UR  - https://www.nature.com/articles/s41467-024-46761-3
N2  - 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.
ER  -

MORICI, Martino; Sara GABRIELLI; Keigo FUJIWARA; Helge PATERNOGA; Bertrand BECKERT; Lars V BOCK; Shinobu CHIBA a Daniel N WILSON. RAPP-containing arrest peptides induce translational stalling by short circuiting the ribosomal peptidyltransferase activity. \textit{Nature Communications}. Berlin: Nature, 2024, roč.~15, č.~1, s.~1-16. ISSN~2041-1723. Dostupné z: https://doi.org/10.1038/s41467-024-46761-3.

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