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Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius

Research output: Contribution to Journal/Magazine › Journal article › peer-review

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Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius. / Anjum, Rana S.; Bray, Sian M.; Blackwood, John K. et al.
In: Nature Communications, Vol. 6, 8163, 08.09.2015.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Anjum, RS, Bray, SM, Blackwood, JK, Kilkenny, ML, Coelho, MA, Foster, BM, Li, S, Howard, JA, Pellegrini, L, Albers, S-V, Deery, MJ & Robinson, NP 2015, 'Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius', Nature Communications, vol. 6, 8163. https://doi.org/10.1038/ncomms9163

APA

Anjum, R. S., Bray, S. M., Blackwood, J. K., Kilkenny, M. L., Coelho, M. A., Foster, B. M., Li, S., Howard, J. A., Pellegrini, L., Albers, S.-V., Deery, M. J., & Robinson, N. P. (2015). Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius. Nature Communications, 6, Article 8163. https://doi.org/10.1038/ncomms9163

Vancouver

Anjum RS, Bray SM, Blackwood JK, Kilkenny ML, Coelho MA, Foster BM et al. Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius. Nature Communications. 2015 Sept 8;6:8163. doi: 10.1038/ncomms9163

Author

Anjum, Rana S. ; Bray, Sian M. ; Blackwood, John K. et al. / Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius. In: Nature Communications. 2015 ; Vol. 6.

Bibtex

@article{c67e7437207f45a6b9c469ee9d7e91f2,
title = "Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius",
abstract = "In eukaryotes, the covalent attachment of ubiquitin chains directs substrates to the proteasome for degradation. Recently, ubiquitin-like modifications have also been described in the archaeal domain of life. It has subsequently been hypothesized that ubiquitin-like proteasomal degradation might also operate in these microbes, since all archaeal species utilize homologues of the eukaryotic proteasome. Here we perform a structural and biochemical analysis of a ubiquitin-like modification pathway in the archaeon Sulfolobus acidocaldarius. We reveal that this modifier is homologous to the eukaryotic ubiquitin-related modifier Urm1, considered to be a close evolutionary relative of the progenitor of all ubiquitin-like proteins. Furthermore we demonstrate that urmylated substrates are recognized and processed by the archaeal proteasome, by virtue of a direct interaction with the modifier. Thus, the regulation of protein stability by Urm1 and the proteasome in archaea is likely representative of an ancient pathway from which eukaryotic ubiquitin-mediated proteolysis has evolved.",
keywords = "Archaeal Proteins, Chromatography, Gel, Chromatography, Liquid, Circular Dichroism, Crystallography, X-Ray, Mass Spectrometry, Microscopy, Electron, Proteasome Endopeptidase Complex, Proteolysis, Sulfolobus acidocaldarius, Ubiquitins, Journal Article, Research Support, Non-U.S. Gov't",
author = "Anjum, {Rana S.} and Bray, {Sian M.} and Blackwood, {John K.} and Kilkenny, {Mairi L.} and Coelho, {Matthew A.} and Foster, {Benjamin M.} and Shurong Li and Howard, {Julie A.} and Luca Pellegrini and Sonja-Verena Albers and Deery, {Michael J.} and Robinson, {Nicholas P.}",
year = "2015",
month = sep,
day = "8",
doi = "10.1038/ncomms9163",
language = "English",
volume = "6",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius

AU - Anjum, Rana S.

AU - Bray, Sian M.

AU - Blackwood, John K.

AU - Kilkenny, Mairi L.

AU - Coelho, Matthew A.

AU - Foster, Benjamin M.

AU - Li, Shurong

AU - Howard, Julie A.

AU - Pellegrini, Luca

AU - Albers, Sonja-Verena

AU - Deery, Michael J.

AU - Robinson, Nicholas P.

PY - 2015/9/8

Y1 - 2015/9/8

N2 - In eukaryotes, the covalent attachment of ubiquitin chains directs substrates to the proteasome for degradation. Recently, ubiquitin-like modifications have also been described in the archaeal domain of life. It has subsequently been hypothesized that ubiquitin-like proteasomal degradation might also operate in these microbes, since all archaeal species utilize homologues of the eukaryotic proteasome. Here we perform a structural and biochemical analysis of a ubiquitin-like modification pathway in the archaeon Sulfolobus acidocaldarius. We reveal that this modifier is homologous to the eukaryotic ubiquitin-related modifier Urm1, considered to be a close evolutionary relative of the progenitor of all ubiquitin-like proteins. Furthermore we demonstrate that urmylated substrates are recognized and processed by the archaeal proteasome, by virtue of a direct interaction with the modifier. Thus, the regulation of protein stability by Urm1 and the proteasome in archaea is likely representative of an ancient pathway from which eukaryotic ubiquitin-mediated proteolysis has evolved.

AB - In eukaryotes, the covalent attachment of ubiquitin chains directs substrates to the proteasome for degradation. Recently, ubiquitin-like modifications have also been described in the archaeal domain of life. It has subsequently been hypothesized that ubiquitin-like proteasomal degradation might also operate in these microbes, since all archaeal species utilize homologues of the eukaryotic proteasome. Here we perform a structural and biochemical analysis of a ubiquitin-like modification pathway in the archaeon Sulfolobus acidocaldarius. We reveal that this modifier is homologous to the eukaryotic ubiquitin-related modifier Urm1, considered to be a close evolutionary relative of the progenitor of all ubiquitin-like proteins. Furthermore we demonstrate that urmylated substrates are recognized and processed by the archaeal proteasome, by virtue of a direct interaction with the modifier. Thus, the regulation of protein stability by Urm1 and the proteasome in archaea is likely representative of an ancient pathway from which eukaryotic ubiquitin-mediated proteolysis has evolved.

KW - Archaeal Proteins

KW - Chromatography, Gel

KW - Chromatography, Liquid

KW - Circular Dichroism

KW - Crystallography, X-Ray

KW - Mass Spectrometry

KW - Microscopy, Electron

KW - Proteasome Endopeptidase Complex

KW - Proteolysis

KW - Sulfolobus acidocaldarius

KW - Ubiquitins

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1038/ncomms9163

DO - 10.1038/ncomms9163

M3 - Journal article

C2 - 26348592

VL - 6

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 8163

ER -