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Functional reconstruction of a eukaryotic-like E1/E2/(RING)E3 ubiquitylation cascade from an uncultured archaeon

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Functional reconstruction of a eukaryotic-like E1/E2/(RING)E3 ubiquitylation cascade from an uncultured archaeon. / James, Rory Hennell; Caceres, Eva F.; Escasinas, Alex et al.
In: Nature Communications, Vol. 8, 1120, 24.10.2017.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

James, RH, Caceres, EF, Escasinas, A, Alhasan, H, Howard, JA, Deery, MJ, Ettema, TJG & Robinson, NP 2017, 'Functional reconstruction of a eukaryotic-like E1/E2/(RING)E3 ubiquitylation cascade from an uncultured archaeon', Nature Communications, vol. 8, 1120. https://doi.org/10.1038/s41467-017-01162-7

APA

James, R. H., Caceres, E. F., Escasinas, A., Alhasan, H., Howard, J. A., Deery, M. J., Ettema, T. J. G., & Robinson, N. P. (2017). Functional reconstruction of a eukaryotic-like E1/E2/(RING)E3 ubiquitylation cascade from an uncultured archaeon. Nature Communications, 8, Article 1120. https://doi.org/10.1038/s41467-017-01162-7

Vancouver

James RH, Caceres EF, Escasinas A, Alhasan H, Howard JA, Deery MJ et al. Functional reconstruction of a eukaryotic-like E1/E2/(RING)E3 ubiquitylation cascade from an uncultured archaeon. Nature Communications. 2017 Oct 24;8:1120. doi: 10.1038/s41467-017-01162-7

Author

James, Rory Hennell ; Caceres, Eva F. ; Escasinas, Alex et al. / Functional reconstruction of a eukaryotic-like E1/E2/(RING)E3 ubiquitylation cascade from an uncultured archaeon. In: Nature Communications. 2017 ; Vol. 8.

Bibtex

@article{ded5fa9b278644dfb1cb8762a128b228,
title = "Functional reconstruction of a eukaryotic-like E1/E2/(RING)E3 ubiquitylation cascade from an uncultured archaeon",
abstract = "The covalent modification of protein substrates by ubiquitin regulates a diverse range of critical biological functions. Although it has been established that ubiquitin-like modifiers evolved from prokaryotic sulphur transfer proteins it is less clear how complex eukaryotic ubiquitylation system arose and diversified from these prokaryotic antecedents. The discovery of ubiquitin, E1-like, E2-like and small-RING finger (srfp) protein components in the Aigarchaeota and the Asgard archaea superphyla has provided a substantive step toward addressing this evolutionary question. Encoded in operons, these components are likely representative of the progenitor apparatus that founded the modern eukaryotic ubiquitin modification systems. Here we report that these proteins from the archaeon Candidatus {\textquoteleft}Caldiarchaeum subterraneum{\textquoteright} operate together as a bona fide ubiquitin modification system, mediating a sequential ubiquitylation cascade reminiscent of the eukaryotic process. Our observations support the hypothesis that complex eukaryotic ubiquitylation signalling pathways have developed from compact systems originally inherited from an archaeal ancestor.",
keywords = "Enzyme mechanisms, Functional clustering, Ubiquitylation",
author = "James, {Rory Hennell} and Caceres, {Eva F.} and Alex Escasinas and Haya Alhasan and Howard, {Julie A.} and Deery, {Michael J.} and Ettema, {Thijs J. G.} and Robinson, {Nicholas Paul}",
year = "2017",
month = oct,
day = "24",
doi = "10.1038/s41467-017-01162-7",
language = "English",
volume = "8",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - Functional reconstruction of a eukaryotic-like E1/E2/(RING)E3 ubiquitylation cascade from an uncultured archaeon

AU - James, Rory Hennell

AU - Caceres, Eva F.

AU - Escasinas, Alex

AU - Alhasan, Haya

AU - Howard, Julie A.

AU - Deery, Michael J.

AU - Ettema, Thijs J. G.

AU - Robinson, Nicholas Paul

PY - 2017/10/24

Y1 - 2017/10/24

N2 - The covalent modification of protein substrates by ubiquitin regulates a diverse range of critical biological functions. Although it has been established that ubiquitin-like modifiers evolved from prokaryotic sulphur transfer proteins it is less clear how complex eukaryotic ubiquitylation system arose and diversified from these prokaryotic antecedents. The discovery of ubiquitin, E1-like, E2-like and small-RING finger (srfp) protein components in the Aigarchaeota and the Asgard archaea superphyla has provided a substantive step toward addressing this evolutionary question. Encoded in operons, these components are likely representative of the progenitor apparatus that founded the modern eukaryotic ubiquitin modification systems. Here we report that these proteins from the archaeon Candidatus ‘Caldiarchaeum subterraneum’ operate together as a bona fide ubiquitin modification system, mediating a sequential ubiquitylation cascade reminiscent of the eukaryotic process. Our observations support the hypothesis that complex eukaryotic ubiquitylation signalling pathways have developed from compact systems originally inherited from an archaeal ancestor.

AB - The covalent modification of protein substrates by ubiquitin regulates a diverse range of critical biological functions. Although it has been established that ubiquitin-like modifiers evolved from prokaryotic sulphur transfer proteins it is less clear how complex eukaryotic ubiquitylation system arose and diversified from these prokaryotic antecedents. The discovery of ubiquitin, E1-like, E2-like and small-RING finger (srfp) protein components in the Aigarchaeota and the Asgard archaea superphyla has provided a substantive step toward addressing this evolutionary question. Encoded in operons, these components are likely representative of the progenitor apparatus that founded the modern eukaryotic ubiquitin modification systems. Here we report that these proteins from the archaeon Candidatus ‘Caldiarchaeum subterraneum’ operate together as a bona fide ubiquitin modification system, mediating a sequential ubiquitylation cascade reminiscent of the eukaryotic process. Our observations support the hypothesis that complex eukaryotic ubiquitylation signalling pathways have developed from compact systems originally inherited from an archaeal ancestor.

KW - Enzyme mechanisms

KW - Functional clustering

KW - Ubiquitylation

U2 - 10.1038/s41467-017-01162-7

DO - 10.1038/s41467-017-01162-7

M3 - Journal article

VL - 8

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 1120

ER -