ArticleNucleic acids research2011
Structural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed.
- Article
- Adaptive genetics reveals constraints on protein structure/function by evolving E. coli under constant nutrient limitation.BMC biology · 2025Article
- Hfq C-terminal region forms a β-rich amyloid-like motif without perturbing the N-terminal Sm-like structure.Communications biology · 2023Article
- Models of Hfq interactions with small non-coding RNA in Gram-negative and Gram-positive bacteria.Frontiers in cellular and infection microbiology · 2023Review
- Catabolite repression control protein antagonist, a novel player inFrontiers in microbiology · 2023Article
- Intrinsically disordered interaction network in an RNA chaperone revealed by native mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- 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
- Stabilization of Hfq-mediated translational repression by the co-repressor Crc in Pseudomonas aeruginosa.Nucleic acids research · 2021Article
- RNA binding of Hfq monomers promotes RelA-mediated hexamerization in a limiting Hfq environment.Nature communications · 2021Article
- Article
- Synchrotron-radiation vacuum-ultraviolet circular dichroism spectroscopy in structural biology: an overview.Biophysics and physicobiology · 2019Review
- Revised role for Hfq bacterial regulator on DNA topology.Scientific reports · 2018Article
- The unusual glycine-rich C terminus of theThe Journal of biological chemistry · 2018Article
- Proteins That Chaperone RNA Regulation.Microbiology spectrum · 2018Review
- Hfq chaperone brings speed dating to bacterial sRNA.Wiley interdisciplinary reviews. RNA · 2018Review
- Interplay between the catabolite repression control protein Crc, Hfq and RNA in Hfq-dependent translational regulation in Pseudomonas aeruginosa.Nucleic acids research · 2018Article
- Membrane association of the bacterial riboregulator Hfq and functional perspectives.Scientific reports · 2017Article
- Intermolecular base stacking mediates RNA-RNA interaction in a crystal structure of the RNA chaperone Hfq.Scientific reports · 2017Article
- Article
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14 authors.
Funding
Abstract
The hexameric Escherichia coli RNA chaperone Hfq (Hfq(Ec)) is involved in riboregulation of target mRNAs by small trans-encoded RNAs. Hfq proteins of different bacteria comprise an evolutionarily conserved core, whereas the C-terminus is variable in length. Although the structure of the conserved core has been elucidated for several Hfq proteins, no structural information has yet been obtained for the C-terminus. Using bioinformatics, nuclear magnetic resonance spectroscopy, synchrotron radiation circular dichroism (SRCD) spectroscopy and small angle X-ray scattering we provide for the first time insights into the conformation and dynamic properties of the C-terminal extension of Hfq(Ec). These studies indicate that the C-termini are flexible and extend laterally away from the hexameric core, displaying in this way features typical of intrinsically disordered proteins that facilitate intermolecular interactions. We identified a minimal, intrinsically disordered region of the C-terminus supporting the interactions with longer RNA fragments. This minimal region together with rest of the C-terminal extension provides a flexible moiety capable of tethering long and structurally diverse RNA molecules. Furthermore, SRCD spectroscopy supported the hypothesis that RNA fragments exceeding a certain length interact with the C-termini of Hfq(Ec).
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