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Title | Perturbed N-glycosylation of Halobacterium salinarum archaellum filaments leads to filament bundling and compromised cell motility. |
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Journal, issue, pages | Nat Commun, Vol. 15, Issue 1, Page 5841, Year 2024 |
Publish date | Jul 11, 2024 |
Authors | Shahar Sofer / Zlata Vershinin / Leen Mashni / Ran Zalk / Anat Shahar / Jerry Eichler / Iris Grossman-Haham / |
PubMed Abstract | 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 ...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 links | Nat Commun / PubMed:38992036 / PubMed Central |
Methods | EM (helical sym.) |
Resolution | 3.06 - 3.33 Å |
Structure data | EMDB-19905, PDB-9eq7: EMDB-19943, PDB-9esm: EMDB-19962, PDB-9etu: |
Source |
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Keywords | STRUCTURAL PROTEIN / archaellum / haloarcheon / archaellin |