ArticleNature communications2017
Signal recognition particle prevents N-terminal processing of bacterial membrane proteins.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- N-terminal formylmethionine as a degron and a specific signal in proteostasis and stress adaptation.Experimental & molecular medicine · 2026Review
- Decreasing peptide deformylase activity is a beneficial strategy for increasing formaldehyde resistance inbioRxiv : the preprint server for biology · 2026Article
- Identification of the lydiamycin biosynthetic gene cluster in a plant pathogen guides structural revision and identification of molecular target.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Lipopeptide antibiotics disrupt interactions of undecaprenyl phosphate with UptA.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- System-wide analyses reveal essential roles of N-terminal protein modification in bacterial membrane integrity.iScience · 2022Article
- Ribosome-nascent Chain Interaction Regulates N-terminal Protein Modification.Journal of molecular biology · 2022Article
- Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022Review
- Kinetic control of nascent protein biogenesis by peptide deformylase.Scientific reports · 2021Article
- Rapid MRSA detection via tandem mass spectrometry of the intact 80 kDa PBP2a resistance protein.Scientific reports · 2021Article
- Mechanisms of Cotranslational Protein Maturation in Bacteria.Frontiers in molecular biosciences · 2021Review
- Timing and specificity of cotranslational nascent protein modification in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Molecular Mimicry of SecA and Signal Recognition Particle Binding to the Bacterial Ribosome.mBio · 2019Article
- Total synthesis of (±)-fumimycin and analogues for biological evaluation as peptide deformylase inhibitors.Tetrahedron · 2019Article
- Cotranslational protein targeting to the membrane: Nascent-chain transfer in a quaternary complex formed at the translocon.Scientific reports · 2018Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial proteins are synthesized with an N-formylated amino-terminal methionine, and N-formylated peptides elicit innate-immunity responses against bacterial infections. However, the source of these formylated peptides is not clear, as most bacterial proteins are co-translationally deformylated by peptide deformylase. Here we develop a deformylation assay with translating ribosomes as substrates, to show that the binding of the signal recognition particle (SRP) to signal sequences in nascent proteins on the ribosome prevents deformylation, whereas deformylation of nascent proteins without signal sequence is not affected. Deformylation and its inhibition by SRP are not influenced by trigger factor, a chaperone that interacts with nascent chains on the ribosome. We propose that bacterial inner-membrane proteins, in particular those with N-out topology, can retain their N-terminal formyl group during cotranslational membrane insertion and supply formylated peptides during bacterial infections.
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