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The evolution of archaeal flagellar filaments.
Kreutzberger, Mark A B; Cvirkaite-Krupovic, Virginija; Liu, Ying; Baquero, Diana P; Liu, Junfeng; Sonani, Ravi R; Calladine, Chris R; Wang, Fengbin; Krupovic, Mart; Egelman, Edward H.
Afiliación
  • Kreutzberger MAB; Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22903.
  • Cvirkaite-Krupovic V; Institut Pasteur, Université Paris Cité, CNRS UMR6047, Archaeal Virology Unit, Paris 75015, France.
  • Liu Y; Institut Pasteur, Université Paris Cité, CNRS UMR6047, Archaeal Virology Unit, Paris 75015, France.
  • Baquero DP; Institut Pasteur, Université Paris Cité, CNRS UMR6047, Archaeal Virology Unit, Paris 75015, France.
  • Liu J; Institut Pasteur, Université Paris Cité, CNRS UMR6047, Archaeal Virology Unit, Paris 75015, France.
  • Sonani RR; Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22903.
  • Calladine CR; Department of Engineering, University of Cambridge, Cambridge CB2 1PZ, United Kingdom.
  • Wang F; Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22903.
  • Krupovic M; Institut Pasteur, Université Paris Cité, CNRS UMR6047, Archaeal Virology Unit, Paris 75015, France.
  • Egelman EH; Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22903.
Proc Natl Acad Sci U S A ; 120(28): e2304256120, 2023 07 11.
Article en En | MEDLINE | ID: mdl-37399404
Flagellar motility has independently arisen three times during evolution: in bacteria, archaea, and eukaryotes. In prokaryotes, the supercoiled flagellar filaments are composed largely of a single protein, bacterial or archaeal flagellin, although these two proteins are not homologous, while in eukaryotes, the flagellum contains hundreds of proteins. Archaeal flagellin and archaeal type IV pilin are homologous, but how archaeal flagellar filaments (AFFs) and archaeal type IV pili (AT4Ps) diverged is not understood, in part, due to the paucity of structures for AFFs and AT4Ps. Despite having similar structures, AFFs supercoil, while AT4Ps do not, and supercoiling is essential for the function of AFFs. We used cryo-electron microscopy to determine the atomic structure of two additional AT4Ps and reanalyzed previous structures. We find that all AFFs have a prominent 10-strand packing, while AT4Ps show a striking structural diversity in their subunit packing. A clear distinction between all AFF and all AT4P structures involves the extension of the N-terminal α-helix with polar residues in the AFFs. Additionally, we characterize a flagellar-like AT4P from Pyrobaculum calidifontis with filament and subunit structure similar to that of AFFs which can be viewed as an evolutionary link, showing how the structural diversity of AT4Ps likely allowed for an AT4P to evolve into a supercoiling AFF.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Archaea / Flagelina Idioma: En Revista: Proc Natl Acad Sci U S A Año: 2023 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Archaea / Flagelina Idioma: En Revista: Proc Natl Acad Sci U S A Año: 2023 Tipo del documento: Article Pais de publicación: Estados Unidos