ArticleNucleic acids research2015
Structural insights into the recognition of the internal A-rich linker from OxyS sRNA by Escherichia coli Hfq.
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 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Spatial arrangement of functional domains in OxyS stress response sRNA.RNA (New York, N.Y.) · 2023Article
- Article
- Dynamic Refolding of OxyS sRNA by the Hfq RNA Chaperone.Journal of molecular biology · 2022Article
- Computational Insights into the Binding Mechanism of OxyS sRNA with Chaperone Protein Hfq.Biomolecules · 2021Article
- Differential Chromosome- and Plasmid-Borne Resistance ofInternational journal of molecular sciences · 2021Article
- Specific and Global RNA Regulators inInternational journal of molecular sciences · 2021Review
- Profiles of Small Regulatory RNAs at Different Growth Phases ofFrontiers in microbiology · 2021Article
- Intermolecular base stacking mediates RNA-RNA interaction in a crystal structure of the RNA chaperone Hfq.Scientific reports · 2017Article
- A Genome-Wide Prediction and Identification of Intergenic Small RNAs by Comparative Analysis inFrontiers in microbiology · 2017Article
- RNA systems biology: uniting functional discoveries and structural tools to understand global roles of RNAs.Current opinion in biotechnology · 2016Review
- Hfq: the flexible RNA matchmaker.Current opinion in microbiology · 2016Review
- MD simulations reveal the basis for dynamic assembly of Hfq-RNA complexes.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Small RNA OxyS is induced during oxidative stress in Escherichia coli and it is an Hfq-dependent negative regulator of mRNA translation. OxyS represses the translation of fhlA and rpoS mRNA, which encode the transcriptional activator and σ(s) subunit of RNA polymerase, respectively. However, little is known regarding how Hfq, an RNA chaperone, interacts with OxyS at the atomic level. Here, using fluorescence polarization and tryptophan fluorescence quenching assays, we verified that the A-rich linker region of OxyS sRNA binds Hfq at its distal side. We also report two crystal structures of Hfq in complex with A-rich RNA fragments from this linker region. Both of these RNA fragments bind to the distal side of Hfq and adopt a different conformation compared with those previously reported for the (A-R-N)n tripartite recognition motif. Furthermore, using fluorescence polarization, electrophoresis mobility shift assays and in vivo translation assays, we found that an Hfq mutant, N48A, increases the binding affinity of OxyS for Hfq in vitro but is defective in the negative regulation of fhlA translation in vivo, suggesting that the normal function of OxyS depends on the details of the interaction with Hfq that may be related to the rapid recycling of Hfq in the cell.
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