ArticleRNA (New York, N.Y.)2014
Recognition of U-rich RNA by Hfq from the Gram-positive pathogen Listeria monocytogenes.
Article in RNA (New York, N.Y.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
24 citing papers in PubMed, 34 citations in OpenAlex.
- KH-R3H domain cooperation in RNA recognition by the global RNA-binding protein KhpB.Nature communications · 2025Article
- The LSmAD Domain of Ataxin-2 Modulates the Structure and RNA Binding of Its Preceding LSm Domain.Cells · 2025Article
- Models of Hfq interactions with small non-coding RNA in Gram-negative and Gram-positive bacteria.Frontiers in cellular and infection microbiology · 2023Review
- Article
- Computational Insights into the Binding Mechanism of OxyS sRNA with Chaperone Protein Hfq.Biomolecules · 2021Article
- The Amyloid Region of Hfq Riboregulator Promotes DsrA:Biology · 2021Article
- S1 Domain RNA-Binding Protein CvfD Is a New Posttranscriptional Regulator That Mediates Cold Sensitivity, Phosphate Transport, and Virulence in Streptococcus pneumoniae D39.Journal of bacteriology · 2020Article
- Crystal structure of an Escherichia coli Hfq Core (residues 2-69)-DNA complex reveals multifunctional nucleic acid binding sites.Nucleic acids research · 2020Article
- Article
- Mycobacterium tuberculosis 6C sRNA binds multiple mRNA targets via C-rich loops independent of RNA chaperones.Nucleic acids research · 2019Article
- Hfq chaperone brings speed dating to bacterial sRNA.Wiley interdisciplinary reviews. RNA · 2018Review
- Article
- ProQ/FinO-domain proteins: another ubiquitous family of RNA matchmakers?Molecular microbiology · 2017Review
- Crystal structure and RNA-binding properties of an Hfq homolog from the deep-branching Aquificae: conservation of the lateral RNA-binding mode.Acta crystallographica. Section D, Structural biology · 2017Article
- Article
- Hfq assists small RNAs in binding to the coding sequence of ompD mRNA and in rearranging its structure.RNA (New York, N.Y.) · 2016Article
- Arginine Patch Predicts the RNA Annealing Activity of Hfq from Gram-Negative and Gram-Positive Bacteria.Journal of molecular biology · 2016Article
- Hfq: the flexible RNA matchmaker.Current opinion in microbiology · 2016Review
- Identification of Novel Immunogenic Proteins of Neisseria gonorrhoeae by Phage Display.PloS one · 2016Article
- Multicomponent mixtures for cryoprotection and ligand solubilization.Biotechnology reports (Amsterdam, Netherlands) · 2015Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Hfq is a post-transcriptional regulator that binds U- and A-rich regions of sRNAs and their target mRNAs to stimulate their annealing in order to effect translation regulation and, often, to alter their stability. The functional importance of Hfq and its RNA-binding properties are relatively well understood in Gram-negative bacteria, whereas less is known about the RNA-binding properties of this riboregulator in Gram-positive species. Here, we describe the structure of Hfq from the Gram-positive pathogen Listeria monocytogenes in its RNA-free form and in complex with a U6 oligoribonucleotide. As expected, the protein takes the canonical hexameric toroidal shape of all other known Hfq structures. The U6 RNA binds on the "proximal face" in a pocket formed by conserved residues Q9, N42, F43, and K58. Additionally residues G5 and Q6 are involved in protein-nucleic and inter-subunit contacts that promote uracil specificity. Unlike Staphylococcus aureus (Sa) Hfq, Lm Hfq requires magnesium to bind U6 with high affinity. In contrast, the longer oligo-uridine, U16, binds Lm Hfq tightly in the presence or absence of magnesium, thereby suggesting the importance of additional residues on the proximal face and possibly the lateral rim in RNA interaction. Intrinsic tryptophan fluorescence quenching (TFQ) studies reveal, surprisingly, that Lm Hfq can bind (GU)3G and U6 on its proximal and distal faces, indicating a less stringent adenine-nucleotide specificity site on the distal face as compared to the Gram-positive Hfq proteins from Sa and Bacillus subtilis and suggesting as yet uncharacterized RNA-binding modes on both faces.
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