par Wien, Frank;Martinez, Denis;Le Brun, Etienne;Jones, Nykola N.C.;Hoffmann, Søren Vrønning;Waeytens, Jehan ;Berbon, Melanie;Habenstein, Birgit;Arluison, Véronique
Référence Microorganisms, 7, 12, 639
Publication Publié, 2019-12
Référence Microorganisms, 7, 12, 639
Publication Publié, 2019-12
Article révisé par les pairs
Résumé : | 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. |