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Open AccessArticle

The Bacterial Amyloid-Like Hfq Promotes In Vitro DNA Alignment

1
Synchrotron SOLEIL, 91192 Gif-sur-Yvette, France
2
Institute of Chemistry and Biology of Membranes and Nano-objects, CBMN UMR5248 CNRS Université de Bordeaux INP, 33607 Pessac, France
3
Laboratoire Léon Brillouin LLB, CEA, CNRS UMR12, Université Paris Saclay, CEA Saclay, 91191 Gif-sur-Yvette, France
4
ISA, Department of Physics and Astronomy, Aarhus University, 8000 Aarhus C, Denmark
5
Structure et Fonction des Membranes Biologiques, Université libre de Bruxelles, B1050 Bruxelles, Belgique
6
Laboratoire de Chimie Physique d’Orsay, CNRS UMR8000, Université Paris-Sud, Université Paris-Saclay 91400 Orsay, France
7
Université de Paris, UFR Sciences du vivant, 35 rue Hélène Brion, 75205 Paris cedex, France
*
Authors to whom correspondence should be addressed.
Microorganisms 2019, 7(12), 639; https://doi.org/10.3390/microorganisms7120639
Received: 26 October 2019 / Revised: 25 November 2019 / Accepted: 28 November 2019 / Published: 3 December 2019
The Hfq protein is reported to be involved in environmental adaptation and virulence of several bacteria. In Gram-negative bacteria, Hfq mediates the interaction between regulatory noncoding RNAs and their target mRNAs. Besides these RNA-related functions, Hfq is also associated with DNA and is a part of the bacterial chromatin. Its precise role in DNA structuration is, however, unclear and whether Hfq plays a direct role in DNA-related processes such as replication or recombination is controversial. In previous works, we showed that Escherichia coli Hfq, or more precisely its amyloid-like C-terminal region (CTR), induces DNA compaction into a condensed form. In this paper, we evidence a new property for Hfq; precisely we show that its CTR influences double helix structure and base tilting, resulting in a strong local alignment of nucleoprotein Hfq:DNA fibers. The significance of this alignment is discussed in terms of chromatin structuration and possible functional consequences on evolutionary processes and adaptation to environment. View Full-Text
Keywords: Nucleoid-associated protein (NAP); DNA compaction; DNA recombination; amyloid; Sm protein; Synchrotron Radiation Circular and Linear Dichroism (SRCD/SRLD); Couette flow cell; atomic force microscopy (AFM); solid state NMR (ssNMR) Nucleoid-associated protein (NAP); DNA compaction; DNA recombination; amyloid; Sm protein; Synchrotron Radiation Circular and Linear Dichroism (SRCD/SRLD); Couette flow cell; atomic force microscopy (AFM); solid state NMR (ssNMR)
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MDPI and ACS Style

Wien, F.; Martinez, D.; Le Brun, E.; Jones, N.C.; Vrønning Hoffmann, S.; Waeytens, J.; Berbon, M.; Habenstein, B.; Arluison, V. The Bacterial Amyloid-Like Hfq Promotes In Vitro DNA Alignment. Microorganisms 2019, 7, 639. https://doi.org/10.3390/microorganisms7120639

AMA Style

Wien F, Martinez D, Le Brun E, Jones NC, Vrønning Hoffmann S, Waeytens J, Berbon M, Habenstein B, Arluison V. The Bacterial Amyloid-Like Hfq Promotes In Vitro DNA Alignment. Microorganisms. 2019; 7(12):639. https://doi.org/10.3390/microorganisms7120639

Chicago/Turabian Style

Wien, Frank; Martinez, Denis; Le Brun, Etienne; Jones, Nykola C.; Vrønning Hoffmann, Søren; Waeytens, Jehan; Berbon, Melanie; Habenstein, Birgit; Arluison, Véronique. 2019. "The Bacterial Amyloid-Like Hfq Promotes In Vitro DNA Alignment" Microorganisms 7, no. 12: 639. https://doi.org/10.3390/microorganisms7120639

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