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TitleThe SecM arrest peptide traps a pre-peptide bond formation state of the ribosome.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 2431, Year 2024
Publish dateMar 19, 2024
AuthorsFelix Gersteuer / Martino Morici / Sara Gabrielli / Keigo Fujiwara / Haaris A Safdari / Helge Paternoga / Lars V Bock / Shinobu Chiba / Daniel N Wilson /
PubMed AbstractNascent polypeptide chains can induce translational stalling to regulate gene expression. This is exemplified by the E. coli secretion monitor (SecM) arrest peptide that induces translational ...Nascent polypeptide chains can induce translational stalling to regulate gene expression. This is exemplified by the E. coli secretion monitor (SecM) arrest peptide that induces translational stalling to regulate expression of the downstream encoded SecA, an ATPase that co-operates with the SecYEG translocon to facilitate insertion of proteins into or through the cytoplasmic membrane. Here we present the structure of a ribosome stalled during translation of the full-length E. coli SecM arrest peptide at 2.0 Å resolution. The structure reveals that SecM arrests translation by stabilizing the Pro-tRNA in the A-site, but in a manner that prevents peptide bond formation with the SecM-peptidyl-tRNA in the P-site. By employing molecular dynamic simulations, we also provide insight into how a pulling force on the SecM nascent chain can relieve the SecM-mediated translation arrest. Collectively, the mechanisms determined here for SecM arrest and relief are also likely to be applicable for a variety of other arrest peptides that regulate components of the protein localization machinery identified across a wide range of bacteria lineages.
External linksNat Commun / PubMed:38503753 / PubMed Central
MethodsEM (single particle)
Resolution2.0 - 2.6 Å
Structure data

18534

8qoa

EMDB-18534, PDB-8qoa:
Structure of SecM-stalled Escherichia coli 70S ribosome
Method: EM (single particle) / Resolution: 2.0 Å

EMDB-18590: Cryo-EM map of rotated SecM-stalled Escherichia coli 70S ribosome
Method: EM (single particle) / Resolution: 2.6 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-PRO:
PROLINE / Proline

ChemComp-HOH:
WATER / Water

Source
  • escherichia coli bw25113 (bacteria)
KeywordsRIBOSOME / SecM / SRC / Stalling / Arrest Peptide / Arrest Motive / Stalling Motive / Stalled Ribosome Complex / SecA / Secretion Monitor / Leader Peptide / TRANSLATION

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