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TitleStructure of a functional archaellum in Bacteria of the Chloroflexota phylum.
Journal, issue, pagesNat Microbiol, Vol. 10, Issue 10, Page 2412-2424, Year 2025
Publish dateSep 17, 2025
AuthorsShamphavi Sivabalasarma / Najwa Taib / Clara L Mollat / Marie Joest / Stefan Steimle / Simonetta Gribaldo / Sonja-Verena Albers /
PubMed AbstractMotility in Archaea is driven by the archaellum, a rotary ATP-driven machinery unrelated to the bacterial flagellum. To date, archaella have been described exclusively in archaea; however, recent ...Motility in Archaea is driven by the archaellum, a rotary ATP-driven machinery unrelated to the bacterial flagellum. To date, archaella have been described exclusively in archaea; however, recent work reported archaellum genes in bacterial strains of the SAR202 clade (Chloroflexota). Here, using MacSyFinder, we show that bona fide archaellum gene clusters are widespread in several members of the Chloroflexota. Analysis of archaellum-encoding loci and Alphafold3-predicted structures show similarity to the archaellum machinery. Using cryo electron microscopy single-particle analysis, we solved the structure of the bacterial archaellum from Litorilinea aerophila to 2.7 Å. We also show the expression and assembly of this machinery in bacteria and its function in swimming motility. Finally, a phylogenomic analysis revealed two horizontal gene transfer events from euryarchaeal members to Chloroflexota. In summary, our study shows that a functional and assembled archaellum machinery can be exchanged between the two prokaryotic domains.
External linksNat Microbiol / PubMed:40962902 / PubMed Central
MethodsEM (helical sym.) / EM (single particle)
Resolution2.7 - 3.4 Å
Structure data

54927

9sie

EMDB-54927, PDB-9sie:
Structure of the bacterial archaellum from L. aerophila
Method: EM (helical sym.) / Resolution: 2.7 Å

54928

9sii

EMDB-54928, PDB-9sii:
Supercoiling bacterial archaellum filament from L. aerophila
Method: EM (single particle) / Resolution: 3.4 Å

Source
  • litorilinea aerophila (bacteria)
KeywordsPROTEIN FIBRIL / Helical / cell surface structure / motility / archaellum / Supercoiling / Superhelicity

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