The Tubular Sheaths Encasing Methanosaeta thermophila Filaments Are Functional Amyloids
| Autor: | Gunna Christiansen, Poul Larsen, Andreas Bøggild, Per Halkjær Nielsen, Marcel Stenvang, Daniel E. Otzen, Kai Finster, Morten Simonsen Dueholm, Brian S. Vad |
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| Rok vydání: | 2015 |
| Předmět: |
Amyloid
Proteases medicine.diagnostic_test Proteolysis Cell Biology Methanosarcinales Biology biology.organism_classification Microbiology Biochemistry Cell wall Microscopy Electron Transmission Tandem Mass Spectrometry mental disorders Biophysics Extracellular medicine Extreme environment Protein folding Molecular Biology Archaea |
| Zdroj: | Dueholm, M S, Larsen, P, Finster, K, Stenvang, M R, Christiansen, G, Vad, B S, Bøggild, A, Otzen, D E & Nielsen, P H 2015, ' The Tubular Sheaths Encasing Methanosaeta thermophila Filaments Are Functional Amyloids ', Journal of Biological Chemistry, vol. 290, no. 33, pp. 20590-20600 . https://doi.org/10.1074/jbc.M115.654780 Dueholm, M S, Larsen, P, Finster, K, Stenvang, M R, Christiansen, G, Vad, B S, Bøggild, A, Otzen, D E & Halkjær Nielsen, P 2015, ' The Tubular Sheaths Encasing Methanosaeta thermophila Filaments are Functional Amyloids ', Journal of Biological Chemistry, vol. 290, pp. 20590-26600 . https://doi.org/10.1074/jbc.M115.654780 |
| ISSN: | 0021-9258 |
| Popis: | 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 that 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 amyloids do not share homology with any of the currently known functional amyloids and clearly represent a new function of the amyloid protein fold. |
| Databáze: | OpenAIRE |
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