Evidence map›Paper›PMID 26348592›Full record

ArticleNature communications2015

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

Rana S Anjum, Sian M Bray, John K Blackwood, Mairi L Kilkenny, Matthew A Coelho, Benjamin M Foster, Shurong Li, Julie A Howard, Luca Pellegrini, Sonja-Verena Albers and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.1field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
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  7. Urm1, not quite a ubiquitin-like modifier?Microbial cell (Graz, Austria) · 2021
    Article
  8. Article
  9. Urm1: A Non-Canonical UBL.Biomolecules · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Early Response ofFrontiers in microbiology · 2018
    Article
  16. Article
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  18. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 2 institutions in 2 countries.

Rana S AnjumDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Sian M BrayDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
John K BlackwoodDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Mairi L KilkennyDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Matthew A CoelhoDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Benjamin M FosterDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Shurong LiDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Julie A HowardDepartment of Biochemistry and Cambridge Systems Biology Centre, Cambridge Centre for Proteomics, Cambridge CB2 1QR, UK.
Luca PellegriniDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Sonja-Verena AlbersMolecular Biology of Archaea, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany.
Michael J DeeryDepartment of Biochemistry and Cambridge Systems Biology Centre, Cambridge Centre for Proteomics, Cambridge CB2 1QR, UK.
Nicholas P RobinsonDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
University of Cambridge · GBMax Planck Institute for Terrestrial Microbiology · DE

Funding

Biotechnology and Biological Sciences Research Council RG53842Medical Research Council G0701443Wellcome Trust 08279/Z/07/ZWellcome Trust 104641
6 · The paper itself

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.

Indexed as

Archaeal ProteinsChromatography, GelChromatography, LiquidCircular DichroismCrystallography, X-RayMass SpectrometryMicroscopy, ElectronProteasome Endopeptidase ComplexProteolysisSulfolobus acidocaldariusUbiquitinsArchaeal ProteinsProteasome Endopeptidase ComplexUbiquitins

Identifiers

PMID26348592
PMCPMC4569737
OpenAlexW1440856081

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.