WIEN, Frank; MARTINEZ, Denis; LE BRUN, Etienne; JONES, Nykola C.; VRONNING HOFFMANN, Soren; WAEYTENS, Jehan; BERBON, Melanie; HABENSTEIN, Birgit; ARLUISON, Veronique

doi:10.3390/microorganisms7120639

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WIEN, Frank

MARTINEZ, Denis

Chimie et Biologie des Membranes et des Nanoobjets [CBMN]

LE BRUN, Etienne

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Microorganisms. 2019, vol. 7, n° 12

Résumé en anglais

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.< Réduire

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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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The Bacterial Amyloid-Like Hfq Promotes In Vitro DNA Alignment

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