ArticleRNA (New York, N.Y.)2003
The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome.
Article in RNA (New York, N.Y.), 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 156 citations in OpenAlex.
- The phenotypic landscape of the model firmicuteProceedings of the National Academy of Sciences of the United States of America · 2026Article
- 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
- Functional diversity and molecular interactions of small membrane proteins in bacteria.microLife · 2025Review
- mRNA targeting eliminates the need for the signal recognition particle during membrane protein insertion in bacteria.Cell reports · 2023Article
- Ribosome selectivity and nascent chain context in modulating the incorporation of fluorescent non-canonical amino acid into proteins.Scientific reports · 2022Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Mechanisms of Cotranslational Protein Maturation in Bacteria.Frontiers in molecular biosciences · 2021Review
- How Quality Control Systems AID Sec-Dependent Protein Translocation.Frontiers in molecular biosciences · 2021Review
- The Perlman syndrome DIS3L2 exoribonuclease safeguards endoplasmic reticulum-targeted mRNA translation and calcium ion homeostasis.Nature communications · 2020Article
- Nascent SecM chain interacts with outer ribosomal surface to stabilize translation arrest.The Biochemical journal · 2020Article
- Timing and specificity of cotranslational nascent protein modification in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Ribosome-Associated Chloroplast SRP54 Enables Efficient Cotranslational Membrane Insertion of Key Photosynthetic Proteins.The Plant cell · 2019Article
- Molecular Mimicry of SecA and Signal Recognition Particle Binding to the Bacterial Ribosome.mBio · 2019Article
- Signal recognition particle binds to translating ribosomes before emergence of a signal anchor sequence.Nucleic acids research · 2017Article
- Rotational restriction of nascent peptides as an essential element of co-translational protein folding: possible molecular players and structural consequences.Biology direct · 2017Article
- Targeting and Insertion of Membrane Proteins.EcoSal Plus · 2017Review
- 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
- Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon.The Journal of cell biology · 2015Article
- Arabidopsis thaliana mutants lacking cpFtsY or cpSRP54 exhibit different defects in photosystem II repair.Frontiers in plant science · 2015Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The signal recognition particle (SRP) from Escherichia coli, composed of Ffh protein and 4.5S RNA, mediates membrane targeting of translating ribosomes displaying a signal or signal-anchor sequence. SRP binds at the peptide exit of the large ribosomal subunit. Structural details of the interaction are not known. Here, the position of Ffh or SRP on the ribosome was probed by using site-specific UV-induced crosslinking by p-azidophenacyl bromide (AzP) attached to a number of cysteine residues engineered into surface positions of Ffh. Efficient crosslinking to vacant ribosomes took place from two positions (AzP17 and AzP25) in the N domain of Ffh, both with Ffh and SRP. Both AzP17 and AzP25 were predominantly crosslinked to ribosomal protein L23 that is located at the peptide exit of the 50S subunit. The SRP receptor, FtsY, did not change the crosslink pattern, whereas the presence of a nascent signal peptide on the ribosome resulted in a second crosslink between Ffh(AzP17) and protein L23, indicating that binding to the nascent signal peptide induced a slightly different arrangement of SRP on the ribosome. These results indicate a model of the topographical arrangement of SRP at the peptide exit of the 50S ribosomal subunit.
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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.