ArticleQRB discovery2022
Amyloid-like Hfq interaction with single-stranded DNA: involvement in recombination and replication in
Article in QRB discovery, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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
14 citing papers in PubMed.
- DNA methylation enhances cooperative disentanglement by the Hfq nucleoid-associated protein.European biophysics journal : EBJ · 2026Article
- The Nucleic Acids Circular Dichroism and Fourier Transform Databases NACDDB and NAIRDB: New Tools for RNA Structural Analysis.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Couette Flow Linear Dichroism Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Application of Synchrotron Radiation Circular Dichroism for Structural Analysis of RNAs.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Molecular recognition and structural plasticity in amyloid-nucleic acid complexes.Journal of structural biology · 2025Review
- Bacterial Amyloids as Hubs for Nucleic Acid Interactions: Implications and Mechanisms.International journal of molecular sciences · 2025Review
- The Power Duo: How the Interplay Between Nucleoid-Associated Proteins and Small Noncoding RNAs Orchestrates the Cellular Regulatory Symphony.Molecular microbiology · 2025Review
- Does the Hfq Protein Contribute to RNA Cargo Translocation into Bacterial Outer Membrane Vesicles?Pathogens (Basel, Switzerland) · 2025Article
- Review
- The Role of the Hfq Protein in Bacterial Resistance to Antibiotics: A Narrative Review.Microorganisms · 2025Review
- Host-dependent alteration of the gut microbiota: the role of luminal microRNAs.Microbiome research reports · 2025Review
- Circular and Linear Dichroism for the Analysis of Small Noncoding RNA Properties.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Hfq C-terminal region forms a β-rich amyloid-like motif without perturbing the N-terminal Sm-like structure.Communications biology · 2023Article
- Interactions and Insertion ofInternational journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interactions between proteins and single-stranded DNA (ssDNA) are crucial for many fundamental biological processes, including DNA replication and genetic recombination. Thus, understanding detailed mechanisms of these interactions is necessary to uncover regulatory rules occurring in all living cells. The RNA-binding Hfq is a pleiotropic bacterial regulator that mediates many aspects of nucleic acid metabolism. The protein notably mediates mRNA stability and translation efficiency by using stress-related small regulatory RNA as cofactors. In addition, Hfq helps to compact double-stranded DNA. In this paper, we focused on the action of Hfq on ssDNA. A combination of experimental methodologies, including spectroscopy and molecular imaging, has been used to probe the interactions of Hfq and its amyloid C-terminal region with ssDNA. Our analysis revealed that Hfq binds to ssDNA. Moreover, we demonstrate for the first time that Hfq drastically changes the structure and helical parameters of ssDNA, mainly due to its C-terminal amyloid-like domain. The formation of the nucleoprotein complexes between Hfq and ssDNA unveils important implications for DNA replication and recombination.
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Registered trials
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