ArticleNucleic acids research2015
Structural basis for the interaction of protein S1 with the Escherichia coli ribosome.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 64 citations in OpenAlex.
- Folding the message: mRNA structure as a regulatory layer of human mitochondrial gene expression.Biochimica et biophysica acta. Molecular cell research · 2026Review
- Suppressor analysis inFrontiers in microbiology · 2026Article
- Generation of ribosomal protein S1 mutants for improving of expression of difficult to translate mRNAs.Applied microbiology and biotechnology · 2025Article
- Molecular basis of mRNA delivery to the bacterial ribosome.Science (New York, N.Y.) · 2024Article
- Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.International journal of molecular sciences · 2024Review
- How Dedicated Ribosomes Translate a Leaderless mRNA.Journal of molecular biology · 2024Article
- Structural insight into translation initiation of thebioRxiv : the preprint server for biology · 2023Article
- Perturbation of protein homeostasis brings plastids at the crossroad between repair and dismantling.PLoS genetics · 2023Article
- Structural insights into the binding of bS1 to the ribosome.Nucleic acids research · 2023Article
- Hfq protein and GcvB small RNA tailoring ofRNA biology · 2023Article
- Article
- Switching at the ribosome: riboswitches need rProteins as modulators to regulate translation.Nature communications · 2021Article
- Macromolecular assemblies supporting transcription-translation coupling.Transcription · 2021Review
- NMR structure of the Vibrio vulnificus ribosomal protein S1 domains D3 and D4 provides insights into molecular recognition of single-stranded RNAs.Nucleic acids research · 2021Article
- How Many Messenger RNAs Can Be Translated by the START Mechanism?International journal of molecular sciences · 2020Article
- Translational Control by Ribosome Pausing in Bacteria: How a Non-uniform Pace of Translation Affects Protein Production and Folding.Frontiers in microbiology · 2020Review
- Global analysis of protein synthesis in Flavobacterium johnsoniae reveals the use of Kozak-like sequences in diverse bacteria.Nucleic acids research · 2019Article
- Stress response as implemented by hibernating ribosomes: a structural overview.The FEBS journal · 2019Review
- Growth phase-specific changes in the composition of E. coli transcription complexes.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2019Article
- Structural evidence for product stabilization by the ribosomal mRNA helicase.RNA (New York, N.Y.) · 2019Article
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Authors and funding
8 authors at 5 institutions in 3 countries.
Funding
Abstract
In Gram-negative bacteria, the multi-domain protein S1 is essential for translation initiation, as it recruits the mRNA and facilitates its localization in the decoding centre. In sharp contrast to its functional importance, S1 is still lacking from the high-resolution structures available for Escherichia coli and Thermus thermophilus ribosomes and thus the molecular mechanism governing the S1-ribosome interaction has still remained elusive. Here, we present the structure of the N-terminal S1 domain D1 when bound to the ribosome at atomic resolution by using a combination of NMR, X-ray crystallography and cryo-electron microscopy. Together with biochemical assays, the structure reveals that S1 is anchored to the ribosome primarily via a stabilizing π-stacking interaction within the short but conserved N-terminal segment that is flexibly connected to domain D1. This interaction is further stabilized by salt bridges involving the zinc binding pocket of protein S2. Overall, this work provides one hitherto enigmatic piece in the 'ribosome puzzle', namely the detailed molecular insight into the topology of the S1-ribosome interface. Moreover, our data suggest novel mechanisms that have the potential to modulate protein synthesis in response to environmental cues by changing the affinity of S1 for the ribosome.
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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.