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Kai Finster

The Tubular Sheaths Encasing Methanosaeta thermophila Filaments are Functional Amyloids

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Standard

The Tubular Sheaths Encasing Methanosaeta thermophila Filaments are Functional Amyloids. / Dueholm, Morten S; Larsen, Poul; Finster, Kai; Stenvang, Marcel R; Christiansen, Gunna; Vad, Brian S; Bøggild, Andreas; Otzen, Daniel E; Halkjær Nielsen, Per.

I: Journal of Biological Chemistry, Bind 290, 24.06.2015, s. 20590-26600.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Dueholm, MS, Larsen, P, Finster, K, Stenvang, MR, Christiansen, G, Vad, BS, Bøggild, A, Otzen, DE & Halkjær Nielsen, P 2015, 'The Tubular Sheaths Encasing Methanosaeta thermophila Filaments are Functional Amyloids', Journal of Biological Chemistry, bind 290, s. 20590-26600. https://doi.org/10.1074/jbc.M115.654780

APA

Dueholm, M. S., Larsen, P., Finster, K., Stenvang, M. R., Christiansen, G., Vad, B. S., ... Halkjær Nielsen, P. (2015). The Tubular Sheaths Encasing Methanosaeta thermophila Filaments are Functional Amyloids. Journal of Biological Chemistry, 290, 20590-26600. https://doi.org/10.1074/jbc.M115.654780

CBE

Dueholm MS, Larsen P, Finster K, Stenvang MR, Christiansen G, Vad BS, Bøggild A, Otzen DE, Halkjær Nielsen P. 2015. The Tubular Sheaths Encasing Methanosaeta thermophila Filaments are Functional Amyloids. Journal of Biological Chemistry. 290:20590-26600. https://doi.org/10.1074/jbc.M115.654780

MLA

Vancouver

Dueholm MS, Larsen P, Finster K, Stenvang MR, Christiansen G, Vad BS o.a. The Tubular Sheaths Encasing Methanosaeta thermophila Filaments are Functional Amyloids. Journal of Biological Chemistry. 2015 jun 24;290:20590-26600. https://doi.org/10.1074/jbc.M115.654780

Author

Dueholm, Morten S ; Larsen, Poul ; Finster, Kai ; Stenvang, Marcel R ; Christiansen, Gunna ; Vad, Brian S ; Bøggild, Andreas ; Otzen, Daniel E ; Halkjær Nielsen, Per. / The Tubular Sheaths Encasing Methanosaeta thermophila Filaments are Functional Amyloids. I: Journal of Biological Chemistry. 2015 ; Bind 290. s. 20590-26600.

Bibtex

@article{38f3d2049f8042048d32a2c5a9af44f9,
title = "The Tubular Sheaths Encasing Methanosaeta thermophila Filaments are Functional Amyloids",
abstract = "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.",
author = "Dueholm, {Morten S} and Poul Larsen and Kai Finster and Stenvang, {Marcel R} and Gunna Christiansen and Vad, {Brian S} and Andreas B{\o}ggild and Otzen, {Daniel E} and {Halkj{\ae}r Nielsen}, Per",
note = "Copyright {\circledC} 2015, The American Society for Biochemistry and Molecular Biology.",
year = "2015",
month = "6",
day = "24",
doi = "10.1074/jbc.M115.654780",
language = "English",
volume = "290",
pages = "20590--26600",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",

}

RIS

TY - JOUR

T1 - The Tubular Sheaths Encasing Methanosaeta thermophila Filaments are Functional Amyloids

AU - Dueholm, Morten S

AU - Larsen, Poul

AU - Finster, Kai

AU - Stenvang, Marcel R

AU - Christiansen, Gunna

AU - Vad, Brian S

AU - Bøggild, Andreas

AU - Otzen, Daniel E

AU - Halkjær Nielsen, Per

N1 - Copyright © 2015, The American Society for Biochemistry and Molecular Biology.

PY - 2015/6/24

Y1 - 2015/6/24

N2 - 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.

AB - 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.

U2 - 10.1074/jbc.M115.654780

DO - 10.1074/jbc.M115.654780

M3 - Journal article

VL - 290

SP - 20590

EP - 26600

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

ER -