Final published version
Licence: CC BY: Creative Commons Attribution 4.0 International License
Research output: Contribution to Journal/Magazine › Journal article › peer-review
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/Magazine › Journal article › peer-review
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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 -