Evidence map›Paper›PMID 20054389›Full record

ArticleNature2010

Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax volcanii.

Matthew A Humbard, Hugo V Miranda, Jae-Min Lim, David J Krause, Jonathan R Pritz, Guangyin Zhou, Sixue Chen, Lance Wells, Julie A Maupin-Furlow

Abstract read
In one paragraph

Article in Nature, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.

0numbers the graph read from it
0cells of the map it votes in
122citing papers in PubMed
10.5field-weighted citation impact, top 1% 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

122 citing papers in PubMed, 185 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Journal of bacteriology · 2025
    Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Insights into the Lysine Acetylome of the HaloarchaeonAntioxidants (Basel, Switzerland) · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Urm1, not quite a ubiquitin-like modifier?Microbial cell (Graz, Austria) · 2021
    Article

62 more citing papers are in PubMed but not listed here.

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

9 authors at 2 institutions in 1 country.

Matthew A HumbardDepartment of Microbiology and Cell Science, University of Florida, Gainesville, Florida 32611, USA.
Hugo V Miranda
Jae-Min Lim
David J Krause
Jonathan R Pritz
Guangyin Zhou
Sixue Chen
Lance Wells
Julie A Maupin-Furlow
University of Florida · USUniversity of Georgia · US

Funding

ZINC DEFICIENCY &PROTEIN EXPRESSION IN RAT OLFACTORY BULBSP41RR018502 · NCRR · UNIVERSITY OF GEORGIA (UGA) · PI AZADI, PARASTOO · 2003 to 2011
$13.1M
Ubiquitin-like Small Archaeal Protein Modification (SAMPylation)R01GM057498 · NIGMS · UNIVERSITY OF FLORIDA · PI MAUPIN-FURLOW, JULIE A · 2000 to 2024
$4.9M
Establishment of a High Performance UPLC-QSTAR Elite Proteomics Platform at UniveS10RR025418 · NCRR · UNIVERSITY OF FLORIDA · PI CHEN, SIXUE · 2009 to 2009
$326k
NCRR NIH HHS 1S10 RR025418-01NCRR NIH HHS P41 RR018502NCRR NIH HHS S10 RR025418NIGMS NIH HHS R01 GM057498
6 · The paper itself

Abstract

Archaea, one of three major evolutionary lineages of life, encode proteasomes highly related to those of eukaryotes. In contrast, archaeal ubiquitin-like proteins are less conserved and not known to function in protein conjugation. This has complicated our understanding of the origins of ubiquitination and its connection to proteasomes. Here we report two small archaeal modifier proteins, SAMP1 and SAMP2, with a beta-grasp fold and carboxy-terminal diglycine motif similar to ubiquitin, that form protein conjugates in the archaeon Haloferax volcanii. The levels of SAMP-conjugates were altered by nitrogen-limitation and proteasomal gene knockout and spanned various functions including components of the Urm1 pathway. LC-MS/MS-based collision-induced dissociation demonstrated isopeptide bonds between the C-terminal glycine of SAMP2 and the epsilon-amino group of lysines from a number of protein targets and Lys 58 of SAMP2 itself, revealing poly-SAMP chains. The widespread distribution and diversity of pathways modified by SAMPylation suggest that this type of protein conjugation is central to the archaeal lineage.

Indexed as

Amino Acid SequenceArchaeal ProteinsGene DeletionGlycylglycineHaloferax volcaniiImmunoprecipitationMass SpectrometryMolecular Sequence DataNitrogenProteasome Endopeptidase ComplexSequence AlignmentSulfurUbiquitinationUbiquitinsArchaeal ProteinsGlycylglycineNitrogenProteasome Endopeptidase ComplexSulfurUbiquitins

Identifiers

PMID20054389
PMCPMC2872088
OpenAlexW2038828398

What OpenQuestion holds

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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.