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dc.rights.licenseopenen_US
dc.contributor.authorWIEN, Frank
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorMARTINEZ, Denis
dc.contributor.authorLE BRUN, Etienne
dc.contributor.authorJONES, Nykola C.
dc.contributor.authorVRONNING HOFFMANN, Soren
dc.contributor.authorWAEYTENS, Jehan
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorBERBON, Melanie
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHABENSTEIN, Birgit
dc.contributor.authorARLUISON, Veronique
dc.date.accessioned2020-04-22T08:22:27Z
dc.date.available2020-04-22T08:22:27Z
dc.date.issued2019
dc.identifier.issn2076-2607en_US
dc.identifier.otherhttps://www.mdpi.com/2076-2607/7/12/639/s1en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/4330
dc.description.abstractEnThe 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.
dc.language.isoENen_US
dc.subject.enNucleoid-associated protein (NAP)
dc.subject.enDNA compaction; DNA recombination
dc.subject.enamyloid; Sm protein; Synchrotron Radiation Circular and Linear Dichroism (SRCD/SRLD); Couette flow cell
dc.subject.enatomic force microscopy (AFM)
dc.subject.ensolid state NMR (ssNMR)
dc.title.enThe Bacterial Amyloid-Like Hfq Promotes In Vitro DNA Alignment
dc.typeArticle de revueen_US
dc.identifier.doi10.3390/microorganisms7120639en_US
dc.subject.halChimie/Matériauxen_US
bordeaux.journalMicroorganismsen_US
bordeaux.volume7en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248en_US
bordeaux.issue12en_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-02550350
hal.version1
hal.date.transferred2020-04-22T08:22:31Z
hal.exporttrue
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