Cargando…
Electron cryo-microscopy reveals the structure of the archaeal thread filament
Pili are filamentous surface extensions that play roles in bacterial and archaeal cellular processes such as adhesion, biofilm formation, motility, cell-cell communication, DNA uptake and horizontal gene transfer. The model archaeaon Sulfolobus acidocaldarius assembles three filaments of the type-IV...
Autores principales: | , , , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9715654/ https://www.ncbi.nlm.nih.gov/pubmed/36456543 http://dx.doi.org/10.1038/s41467-022-34652-4 |
_version_ | 1784842500769316864 |
---|---|
author | Gaines, Matthew C. Isupov, Michail N. Sivabalasarma, Shamphavi Haque, Risat Ul McLaren, Mathew Mollat, Clara L. Tripp, Patrick Neuhaus, Alexander Gold, Vicki A. M. Albers, Sonja-Verena Daum, Bertram |
author_facet | Gaines, Matthew C. Isupov, Michail N. Sivabalasarma, Shamphavi Haque, Risat Ul McLaren, Mathew Mollat, Clara L. Tripp, Patrick Neuhaus, Alexander Gold, Vicki A. M. Albers, Sonja-Verena Daum, Bertram |
author_sort | Gaines, Matthew C. |
collection | PubMed |
description | Pili are filamentous surface extensions that play roles in bacterial and archaeal cellular processes such as adhesion, biofilm formation, motility, cell-cell communication, DNA uptake and horizontal gene transfer. The model archaeaon Sulfolobus acidocaldarius assembles three filaments of the type-IV pilus superfamily (archaella, archaeal adhesion pili and UV-inducible pili), as well as a so-far uncharacterised fourth filament, named “thread”. Here, we report on the cryo-EM structure of the archaeal thread. The filament is highly glycosylated and consists of subunits of the protein Saci_0406, arranged in a head-to-tail manner. Saci_0406 displays structural similarity, but low sequence homology, to bacterial type-I pilins. Thread subunits are interconnected via donor strand complementation, a feature reminiscent of bacterial chaperone-usher pili. However, despite these similarities in overall architecture, archaeal threads appear to have evolved independently and are likely assembled by a distinct mechanism. |
format | Online Article Text |
id | pubmed-9715654 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-97156542022-12-03 Electron cryo-microscopy reveals the structure of the archaeal thread filament Gaines, Matthew C. Isupov, Michail N. Sivabalasarma, Shamphavi Haque, Risat Ul McLaren, Mathew Mollat, Clara L. Tripp, Patrick Neuhaus, Alexander Gold, Vicki A. M. Albers, Sonja-Verena Daum, Bertram Nat Commun Article Pili are filamentous surface extensions that play roles in bacterial and archaeal cellular processes such as adhesion, biofilm formation, motility, cell-cell communication, DNA uptake and horizontal gene transfer. The model archaeaon Sulfolobus acidocaldarius assembles three filaments of the type-IV pilus superfamily (archaella, archaeal adhesion pili and UV-inducible pili), as well as a so-far uncharacterised fourth filament, named “thread”. Here, we report on the cryo-EM structure of the archaeal thread. The filament is highly glycosylated and consists of subunits of the protein Saci_0406, arranged in a head-to-tail manner. Saci_0406 displays structural similarity, but low sequence homology, to bacterial type-I pilins. Thread subunits are interconnected via donor strand complementation, a feature reminiscent of bacterial chaperone-usher pili. However, despite these similarities in overall architecture, archaeal threads appear to have evolved independently and are likely assembled by a distinct mechanism. Nature Publishing Group UK 2022-12-01 /pmc/articles/PMC9715654/ /pubmed/36456543 http://dx.doi.org/10.1038/s41467-022-34652-4 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Gaines, Matthew C. Isupov, Michail N. Sivabalasarma, Shamphavi Haque, Risat Ul McLaren, Mathew Mollat, Clara L. Tripp, Patrick Neuhaus, Alexander Gold, Vicki A. M. Albers, Sonja-Verena Daum, Bertram Electron cryo-microscopy reveals the structure of the archaeal thread filament |
title | Electron cryo-microscopy reveals the structure of the archaeal thread filament |
title_full | Electron cryo-microscopy reveals the structure of the archaeal thread filament |
title_fullStr | Electron cryo-microscopy reveals the structure of the archaeal thread filament |
title_full_unstemmed | Electron cryo-microscopy reveals the structure of the archaeal thread filament |
title_short | Electron cryo-microscopy reveals the structure of the archaeal thread filament |
title_sort | electron cryo-microscopy reveals the structure of the archaeal thread filament |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9715654/ https://www.ncbi.nlm.nih.gov/pubmed/36456543 http://dx.doi.org/10.1038/s41467-022-34652-4 |
work_keys_str_mv | AT gainesmatthewc electroncryomicroscopyrevealsthestructureofthearchaealthreadfilament AT isupovmichailn electroncryomicroscopyrevealsthestructureofthearchaealthreadfilament AT sivabalasarmashamphavi electroncryomicroscopyrevealsthestructureofthearchaealthreadfilament AT haquerisatul electroncryomicroscopyrevealsthestructureofthearchaealthreadfilament AT mclarenmathew electroncryomicroscopyrevealsthestructureofthearchaealthreadfilament AT mollatclaral electroncryomicroscopyrevealsthestructureofthearchaealthreadfilament AT tripppatrick electroncryomicroscopyrevealsthestructureofthearchaealthreadfilament AT neuhausalexander electroncryomicroscopyrevealsthestructureofthearchaealthreadfilament AT goldvickiam electroncryomicroscopyrevealsthestructureofthearchaealthreadfilament AT alberssonjaverena electroncryomicroscopyrevealsthestructureofthearchaealthreadfilament AT daumbertram electroncryomicroscopyrevealsthestructureofthearchaealthreadfilament |