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Amyloid-like Hfq interaction with single stranded DNA: involvement in recombination and replication in Escherichia coli

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DOI

  • Krzysztof Kubiak, University of Gdansk, Universite Paris-Saclay, Poland
  • Frank Wien, Synchrotron SOLEIL, F-91192 Gif Sur Yvette, France, France
  • Indresh Yadav, National University of Singapore, Singapore
  • Nykola C. Jones
  • Søren Vrønning Hoffmann
  • Eric Le Cam, Universite Paris-Saclay, France
  • Antoine Cossa, Universite Paris-Saclay, France
  • Frederic Geinguenaud, Universite Paris 13, France
  • Johan R. C. van der Maarel, National University of Singapore, Singapore
  • Grzegorz Węgrzyn, University of Gdansk, Poland
  • Veronique Arluison, Universite Paris-Saclay, Université de Paris, France
Interactions between proteins and single stranded DNA (ssDNA) are crucial for many fundamental biological processes, including DNA replication and genetic recombination. Thus, understanding detailed mechanisms of these interactions is necessary to uncover regulatory rules occurring in all living cells. The RNA-binding Hfq is a pleiotropic bacterial regulator that mediates many aspects of nucleic acids metabolism. The protein notably mediates mRNA stability and translation efficiency by using stress-related small regulatory RNA as cofactors. In addition, Hfq helps to compact double stranded DNA. In this paper, we focused on the action of Hfq on ssDNA. A combination of experimental methodologies, including spectroscopy and molecular imaging, have been used to probe the interactions of Hfq and its amyloid C-terminal region with ssDNA. Our analysis revealed that Hfq binds to ssDNA. Moreover, we demonstrate for the first time that Hfq drastically changes the structure and helical parameters of ssDNA, mainly due to its C-terminal amyloid-like domain. The formation of the nucleoprotein complexes between Hfq and ssDNA unveil important implications for DNA replication and recombination.
Original languageEnglish
Article numbere15
JournalQRB Discovery
Volume3
Number of pages10
ISSN2633-2892
DOIs
Publication statusPublished - 2022

    Research areas

  • Hfq, Sm-like protein, bacterial amyloid, non-coding RNA, nucleoid associated protein, single-stranded DNA-binding protein

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