ArticleBioscience reports2015
New insight into the structure and function of Hfq C-terminus.
Article in Bioscience reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
What it found
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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
45 citing papers in PubMed, 75 citations in OpenAlex.
- Dual Role of Small Noncoding RNA and Hfq in Bacterial DNA Compaction: A New Perspective on Nucleoid Architecture.ACS omega · 2026Article
- Uncovering a previously unknown function of polyphosphate in polyadenylated RNA-induced amyloidogenesis of Hfq.The FEBS journal · 2026Article
- RNAs Associated With Bacterial Outer Membrane Vesicles: Structural Insights Into Surface Composition.Journal of extracellular vesicles · 2026Article
- Inelastic Neutron Scattering: Prospects for Measuring Atomic Vibrations of Nucleic Acids.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Mechanisms and Pathological Significance of Liquid-Liquid Phase Separation in Bacteria.FASEB journal : official publication of the Federation of American Societies for Experimental 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
- Amyloid-like DNA bridging: a new mode of DNA shaping.Nucleic acids research · 2025Article
- The Role of the Hfq Protein in Bacterial Resistance to Antibiotics: A Narrative Review.Microorganisms · 2025Review
- The Protein Scaffolding Functions of Polyphosphate.Journal of molecular biology · 2024Review
- Hfq-Antisense RNA I Binding Regulates RNase E-Dependent RNA Stability and ColE1 Plasmid Copy Number.International journal of molecular sciences · 2024Article
- Bacterial nucleoid is a riddle wrapped in a mystery inside an enigma.Journal of bacteriology · 2024Review
- Role of the Bacterial Amyloid-like Hfq in Fluoroquinolone Fluxes.Microorganisms · 2023Article
- 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
- Dynamic Refolding of OxyS sRNA by the Hfq RNA Chaperone.Journal of molecular biology · 2022Article
- Unraveling Membrane Perturbations Caused by the Bacterial Riboregulator Hfq.International journal of molecular sciences · 2022Article
- Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
Accumulating evidence indicates that RNA metabolism components assemble into supramolecular cellular structures to mediate functional compartmentalization within the cytoplasmic membrane of the bacterial cell. This cellular compartmentalization could play important roles in the processes of RNA degradation and maturation. These components include Hfq, the RNA chaperone protein, which is involved in the post-transcriptional control of protein synthesis mainly by the virtue of its interactions with several small regulatory ncRNAs (sRNA). The Escherichia coli Hfq is structurally organized into two domains. An N-terminal domain that folds as strongly bent β-sheets within individual protomers to assemble into a typical toroidal hexameric ring. A C-terminal flexible domain that encompasses approximately one-third of the protein seems intrinsically unstructured. RNA-binding function of Hfq mainly lies within its N-terminal core, whereas the function of the flexible domain remains controversial and largely unknown. In the present study, we demonstrate that the Hfq-C-terminal region (CTR) has an intrinsic property to self-assemble into long amyloid-like fibrillar structures in vitro. We show that normal localization of Hfq within membrane-associated coiled structures in vivo requires this C-terminal domain. This finding establishes for the first time a function for the hitherto puzzling CTR, with a plausible central role in RNA transactions.
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Registered trials
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.