ArticleThe Journal of cell biology2003
Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome.
Article in The Journal of cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 142 citations in OpenAlex.
- The phenotypic landscape of the model firmicuteProceedings of the National Academy of Sciences of the United States of America · 2026Article
- A delayed translocation into the endoplasmic reticulum controls the post-translational modifications of PD-L1.Nature communications · 2026Article
- Multivalent Interactions between Chaperone and Ribosome-Nascent Chain Complex Revealed by High-Speed AFM and MD Simulations.ACS nano · 2025Article
- Dynamic binding of the bacterial chaperone Trigger factor to translating ribosomes inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Nascent chains derived from a foldable protein sequence interact with specific ribosomal surface sites near the exit tunnel.Scientific reports · 2024Article
- Mapping Protein-Protein Interactions at Birth: Single-Particle Cryo-EM Analysis of a Ribosome-Nascent Globin Complex.ACS central science · 2024Article
- Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophysical chemistry · 2022Review
- Ribosome-nascent Chain Interaction Regulates N-terminal Protein Modification.Journal of molecular biology · 2022Article
- An intrinsically disordered nascent protein interacts with specific regions of the ribosomal surface near the exit tunnel.Communications biology · 2021Article
- Fluorescence Anisotropy Decays and Microscale-Volume Viscometry Reveal the Compaction of Ribosome-Bound Nascent Proteins.The journal of physical chemistry. B · 2021Article
- Ribosome-Associated Chloroplast SRP54 Enables Efficient Cotranslational Membrane Insertion of Key Photosynthetic Proteins.The Plant cell · 2019Article
- Biogenesis, quality control, and structural dynamics of proteins as explored in living cells via site-directed photocrosslinking.Protein science : a publication of the Protein Society · 2019Review
- Biogenesis of chloroplast outer envelope membrane proteins.Plant cell reports · 2019Review
- The SRP signal sequence of KdpD.Scientific reports · 2019Article
- MatureP: prediction of secreted proteins with exclusive information from their mature regions.Scientific reports · 2017Article
- Single-molecule dynamics of the molecular chaperone trigger factor in living cells.Molecular microbiology · 2016Article
- Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon.Nature communications · 2016Article
- Regulation by a chaperone improves substrate selectivity during cotranslational protein targeting.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.Cellular and molecular life sciences : CMLS · 2014Review
- Regulation of cargo recognition, commitment, and unloading drives cotranslational protein targeting.The Journal of cell biology · 2014Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
As newly synthesized polypeptides emerge from the ribosome, they interact with chaperones and targeting factors that assist in folding and targeting to the proper location in the cell. In Escherichia coli, the chaperone trigger factor (TF) binds to nascent polypeptides early in biosynthesis facilitated by its affinity for the ribosomal proteins L23 and L29 that are situated around the nascent chain exit site on the ribosome. The targeting factor signal recognition particle (SRP) interacts specifically with the signal anchor (SA) sequence in nascent inner membrane proteins (IMPs). Here, we have used photocross-linking to map interactions of the SA sequence in a short, in vitro-synthesized, nascent IMP. Both TF and SRP were found to interact with the SA with partially overlapping binding specificity. In addition, extensive contacts with L23 and L29 were detected. Both purified TF and SRP could be cross-linked to L23 on nontranslating ribosomes with a competitive advantage for SRP. The results suggest a role for L23 in the targeting of IMPs as an attachment site for TF and SRP that is close to the emerging nascent chain.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.