ArticleProceedings of the National Academy of Sciences of the United States of America2012
Ribosomal protein S1 unwinds double-stranded RNA in multiple steps.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 97 citations in OpenAlex.
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- Reversible acetylation of ribosomal protein S1 serves as a smart switch for Salmonella to rapidly adapt to host stress.Nucleic acids research · 2025Article
- 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
- Bactericidal effect of tetracycline in E. coli strain ED1a may be associated with ribosome dysfunction.Nature communications · 2024Article
- Molecular physiological characterization of the dynamics of persister formation inAntimicrobial agents and chemotherapy · 2024Article
- Comprehensive quantitative modeling of translation efficiency in a genome-reduced bacterium.Molecular systems biology · 2023Article
- Structural insights into the binding of bS1 to the ribosome.Nucleic acids research · 2023Article
- Selective recruitment of stress-responsive mRNAs to ribosomes for translation by acetylated protein S1 during nutrient stress in Escherichia coli.Communications biology · 2022Article
- Incoherent dual regulation by a SAM-II riboswitch controlling translation at a distance.RNA biology · 2022Article
- Ribosomal Hibernation-Associated Factors inMicroorganisms · 2021Review
- The diversity of Shine-Dalgarno sequences sheds light on the evolution of translation initiation.RNA biology · 2021Review
- Simplification of Ribosomes in Bacteria with Tiny Genomes.Molecular biology and evolution · 2021Article
- An RNA pseudoknot is essential for standby-mediated translation of the tisB toxin mRNA in Escherichia coli.Nucleic acids research · 2020Article
- Analysis of translating mitoribosome reveals functional characteristics of translation in mitochondria of fungi.Nature communications · 2020Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
The sequence and secondary structure of the 5'-end of mRNAs regulate translation by controlling ribosome initiation on the mRNA. Ribosomal protein S1 is crucial for ribosome initiation on many natural mRNAs, particularly for those with structured 5'-ends, or with no or weak Shine-Dalgarno sequences. Besides a critical role in translation, S1 has been implicated in several other cellular processes, such as transcription recycling, and the rescuing of stalled ribosomes by tmRNA. The mechanisms of S1 functions are still elusive but have been widely considered to be linked to the affinity of S1 for single-stranded RNA and its corresponding destabilization of mRNA secondary structures. Here, using optical tweezers techniques, we demonstrate that S1 promotes RNA unwinding by binding to the single-stranded RNA formed transiently during the thermal breathing of the RNA base pairs and that S1 dissociation results in RNA rezipping. We measured the dependence of the RNA unwinding and rezipping rates on S1 concentration, and the force applied to the ends of the RNA. We found that each S1 binds 10 nucleotides of RNA in a multistep fashion implying that S1 can facilitate ribosome initiation on structured mRNA by first binding to the single strand next to an RNA duplex structure ("stand-by site") before subsequent binding leads to RNA unwinding. Unwinding by multiple small substeps is much less rate limited by thermal breathing than unwinding in a single step. Thus, a multistep scheme greatly expedites S1 unwinding of an RNA structure compared to a single-step mode.
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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.