title: Effects of Hfq on the conformation and compaction of DNA.
abstract: Hfq is a bacterial pleiotropic regulator that mediates several aspects of nucleic acids metabolism. The protein notably influences translation and turnover of cellular RNAs. Although most previous contributions concentrated on Hfq's interaction with RNA, its association to DNA has also been observed in vitro and in vivo. Here, we focus on DNA-compacting properties of Hfq. Various experimental technologies, including fluorescence microscopy imaging of single DNA molecules confined inside nanofluidic channels, atomic force microscopy and small angle neutron scattering have been used to follow the assembly of Hfq on DNA. Our results show that Hfq forms a nucleoprotein complex, changes the mechanical properties of the double helix and compacts DNA into a condensed form. We propose a compaction mechanism based on protein-mediated bridging of DNA segments. The propensity for bridging is presumably related to multi-arm functionality of the Hfq hexamer, resulting from binding of the C-terminal domains to the duplex. Results are discussed in regard to previous results obtained for H-NS, with important implications for protein binding related gene regulation.
authors.affiliation: Department of Physics, National University of Singapore, 2 Science Drive 3, 117542, Singapore.
authors.forename: Kai
authors.initials: K
authors.lastname: Jiang
authors.affiliation: Department of Physics, National University of Singapore, 2 Science Drive 3, 117542, Singapore.
authors.forename: Ce
authors.initials: C
authors.lastname: Zhang
authors.affiliation: Department of Physics, National University of Singapore, 2 Science Drive 3, 117542, Singapore.
authors.forename: Durgarao
authors.initials: D
authors.lastname: Guttula
authors.affiliation: Department of Physics, National University of Singapore, 2 Science Drive 3, 117542, Singapore.
authors.forename: Fan
authors.initials: F
authors.lastname: Liu
authors.affiliation: Department of Physics, National University of Singapore, 2 Science Drive 3, 117542, Singapore.
authors.forename: Jeroen A
authors.initials: JA
authors.lastname: van Kan
authors.affiliation: Genomes Structure and Instability, Sorbonne Universities, National Museum of Natural History, Inserm U 1154, CNRS UMR 7196, 75005 Paris, France.
authors.forename: Christophe
authors.initials: C
authors.lastname: Lavelle
authors.affiliation: Laboratoire Léon Brillouin, UMR 12 CEA/CNRS, CEA-Saclay, Gif sur Yvette Cedex 91191, France Department of Molecular Biology, University of Gdansk, Wita Stwosza 59, 80-308 Gdansk, Poland.
authors.forename: Krzysztof
authors.initials: K
authors.lastname: Kubiak
authors.affiliation: Laboratoire Léon Brillouin, UMR 12 CEA/CNRS, CEA-Saclay, Gif sur Yvette Cedex 91191, France.
authors.forename: Antoine
authors.initials: A
authors.lastname: Malabirade
authors.affiliation: Laboratoire Léon Brillouin, UMR 12 CEA/CNRS, CEA-Saclay, Gif sur Yvette Cedex 91191, France.
authors.forename: Alain
authors.initials: A
authors.lastname: Lapp
authors.affiliation: Laboratoire Léon Brillouin, UMR 12 CEA/CNRS, CEA-Saclay, Gif sur Yvette Cedex 91191, France Université Paris Diderot, Sorbonne Paris Cité, 75013 Paris, France johanmaarel@gmail.com.
authors.forename: Véronique
authors.initials: V
authors.lastname: Arluison
authors.affiliation: Department of Physics, National University of Singapore, 2 Science Drive 3, 117542, Singapore johanmaarel@gmail.com.
authors.forename: Johan R C
authors.initials: JR
authors.lastname: van der Maarel
mesh_terms: D004247:DNA / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D035001:Host Factor 1 Protein / Q000378:metabolism*; D044085:Microfluidics; D009690:Nucleic Acid Conformation; D011485:Protein Binding
chemical_list: D035001:Host Factor 1 Protein; D004247:DNA
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