-
Uddannelse
Find uddannelse
Studievejledning
Kvalitet
- Forskning
-
Samarbejde
Virksomheder
Kommuner og regioner
Gymnasier
Myndigheder
-
Om AU
Organisation
Kontakt
Om AU
- Organisation
- Ledelse
- Strategi
- AU i tal
- AU's historie
- Internationalt samarbejde
- Bæredygtighed
- Campus 2.0
- Diversitet og ligestilling
- Ledige stillinger
- Presse
- Kontakt
The Tubular Sheaths Encasing Methanosaeta thermophila Filaments are Functional Amyloids
Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review
- Morten S Dueholm, Aalborg Universitet ,
- Poul Larsen, Aalborg Universitet, Danmark
- Kai Finster
- Marcel R Stenvang ,
- Gunna Christiansen ,
- Brian S Vad ,
- Andreas Bøggild
- Daniel E Otzen
- Per Halkjær Nielsen, Aalborg Universitet, Danmark
- Institut for Biologi - Mikrobiologi
- Interdisciplinary Nanoscience Center - INANO-Kemi, iNANO-huset
- Institut for Biomedicin - Forskning og uddannelse, Øst
- Institut for Kemi
- Institut for Molekylærbiologi og Genetik - Strukturel Biologi
- Interdisciplinary Nanoscience Center - INANO-MBG, iNANO-huset
- Institut for Molekylærbiologi og Genetik - Proteinforskning
Archaea are renowned for their ability to thrive in extreme environments, although they can be found in virtually all habitats. Their adaptive success is linked to their unique cell envelopes that are extremely resistant to chemical and thermal denaturation and resist proteolysis by common proteases. Here we employ amyloid-specific conformation antibodies and biophysical techniques to show that the extracellular cell wall sheaths encasing the methanogenic archaea Methanosaeta thermophila PT are functional amyloids. Depolymerization of sheaths and subsequent MS/MS analyses revealed that the sheaths are composed of a single major sheath protein (MspA). The amyloidogenic nature of MspA was confirmed by in vitro amyloid formation of recombinant MspA under a wide range of environmental conditions. This is the first report of a functional amyloid from the archaeal domain of life. The amyloid nature explains the extreme resistance of the sheath, the elastic properties that allow diffusible substrates to penetrate through expandable hoop boundaries, and how the sheaths are able to split and elongate outside the cell. The archaeal sheath amyloid do not share homology with any of the currently known functional amyloids and clearly represent a new function of the amyloid protein fold.
| Originalsprog | Engelsk |
|---|---|
| Tidsskrift | Journal of Biological Chemistry |
| Vol/bind | 290 |
| Sider (fra-til) | 20590-26600 |
| Antal sider | 11 |
| ISSN | 0021-9258 |
| DOI | |
| Status | Udgivet - 24 jun. 2015 |
Se relationer på Aarhus Universitet Citationsformater
ID: 89915986