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TitleAmyloid-like DNA bridging: a new mode of DNA shaping.
Journal, issue, pagesNucleic Acids Res, Vol. 53, Issue 5, Year 2025
Publish dateFeb 27, 2025
AuthorsFrank Wien / Marcos Gragera / Tatsuhito Matsuo / Gautier Moroy / María Teresa Bueno-Carrasco / Rocío Arranz / Antoine Cossa / Anne Martel / Heloisa N Bordallo / Svemir Rudić / Marisela Velez / Johan R C van der Maarel / Judith Peters / Véronique Arluison /
PubMed AbstractAll organisms depend on specific proteins to compact and organize their genomes. In eukaryotes, histones fulfil this role, while bacterial chromosomes are shaped by nucleoid-associated proteins (NAPs) ...All organisms depend on specific proteins to compact and organize their genomes. In eukaryotes, histones fulfil this role, while bacterial chromosomes are shaped by nucleoid-associated proteins (NAPs). Among its pleiotropic functions, the NAP Hfq plays a pivotal role in bacterial genome organization. In this study, we characterized the structure of the C-terminal extension of Hfq, which mediates chromosomal compaction, in its DNA-bound state. Using an integrative approach that combined transmission electron microscopy, neutron scattering, site-directed mutagenesis, and molecular modeling, we identified an amyloid module formed by the C-terminal region of Hfq. This module uniquely bridges and compacts six DNA molecules, marking the first documented instance of an amyloid structure with DNA-bridging properties. Our findings redefine the functional landscape of amyloids, linking them to genome architecture and gene regulation. This result suggests that amyloid-DNA interactions may represent a conserved mechanism across biological systems, with profound implications for understanding genome organization and the regulation of gene expression in both prokaryotes and eukaryotes.
External linksNucleic Acids Res / PubMed:40066879 / PubMed Central
MethodsEM (helical sym.)
Resolution19.0 Å
Structure data

EMDB-52187: Amyloid DNA Bridging by Hfq C-terminal region
Method: EM (helical sym.) / Resolution: 19.0 Å

Source
  • E. coli K12 (bacteria)
  • Escherichia coli (E. coli)
  • synthetic construct (others)

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