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TitlePerturbed N-glycosylation of Halobacterium salinarum archaellum filaments leads to filament bundling and compromised cell motility.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 5841, Year 2024
Publish dateJul 11, 2024
AuthorsShahar Sofer / Zlata Vershinin / Leen Mashni / Ran Zalk / Anat Shahar / Jerry Eichler / Iris Grossman-Haham /
PubMed AbstractThe swimming device of archaea-the archaellum-presents asparagine (N)-linked glycans. While N-glycosylation serves numerous roles in archaea, including enabling their survival in extreme ...The swimming device of archaea-the archaellum-presents asparagine (N)-linked glycans. While N-glycosylation serves numerous roles in archaea, including enabling their survival in extreme environments, how this post-translational modification contributes to cell motility remains under-explored. Here, we report the cryo-EM structure of archaellum filaments from the haloarchaeon Halobacterium salinarum, where archaellins, the building blocks of the archaellum, are N-glycosylated, and the N-glycosylation pathway is well-resolved. We further determined structures of archaellum filaments from two N-glycosylation mutant strains that generate truncated glycans and analyzed their motility. While cells from the parent strain exhibited unidirectional motility, the N-glycosylation mutant strain cells swam in ever-changing directions within a limited area. Although these mutant strain cells presented archaellum filaments that were highly similar in architecture to those of the parent strain, N-linked glycan truncation greatly affected interactions between archaellum filaments, leading to dramatic clustering of both isolated and cell-attached filaments. We propose that the N-linked tetrasaccharides decorating archaellins act as physical spacers that minimize the archaellum filament aggregation that limits cell motility.
External linksNat Commun / PubMed:38992036 / PubMed Central
MethodsEM (helical sym.)
Resolution3.06 - 3.33 Å
Structure data

19905

9eq7

EMDB-19905, PDB-9eq7:
Halobacterium salinarum archaellum filament
Method: EM (helical sym.) / Resolution: 3.23 Å

19943

9esm

EMDB-19943, PDB-9esm:
Archaellum filament from the Halobacterium salinarum deltaAgl26 strain
Method: EM (helical sym.) / Resolution: 3.06 Å

19962

9etu

EMDB-19962, PDB-9etu:
Archaellum filament from the Halobacterium salinarum deltaAgl27 strain
Method: EM (helical sym.) / Resolution: 3.33 Å

Source
  • halobacterium salinarum (Halophile)
KeywordsSTRUCTURAL PROTEIN / archaellum / haloarcheon / archaellin

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