Evidence map›Paper›PMID 17599068›Full record

ArticleThe EMBO journal2007

Sequence and structure evolved separately in a ribosomal ubiquitin variant.

André Catic, Zhen-Yu J Sun, Daniel M Ratner, Shahram Misaghi, Eric Spooner, John Samuelson, Gerhard Wagner, Hidde L Ploegh

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Computational modeling of Repeat1 region of INI1/hSNF5: An evolutionary link with ubiquitin.Protein science : a publication of the Protein Society · 2016
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. The N-end rule pathway and regulation by proteolysis.Protein science : a publication of the Protein Society · 2011
    Review
  12. Article
  13. Article
  14. Article
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

8 authors at 5 institutions in 1 country.

André CaticDepartment of Biology, Whitehead Institute for Biomedical Research and Massachusetts Institute of Technology, Cambridge, MA 02142, USA.
Zhen-Yu J Sun
Daniel M Ratner
Shahram Misaghi
Eric Spooner
John Samuelson
Gerhard Wagner
Hidde L Ploegh
Whitehead Institute for Biomedical Research · USHarvard University · USBoston Medical Center · USBoston University · USMassachusetts Institute of Technology · US

Funding

T CELL SPECIFIC TRANSCRIPTION COMPLEXESP01GM047467 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1992 to 2017
$28.6M
Glycobiology of GiardiaR01AI048082 · NIAID · BOSTON UNIVERSITY MEDICAL CAMPUS · PI SAMUELSON, JOHN C. · 2003 to 2015
$4.0M
STRUCTURAL BASIS OF TRANSLATION INITIATION BY EIF-4ER01CA068262 · NCI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1996 to 2015
$3.6M
Training Program in Host Pathogen InteractionsT32AI052070 · NIAID · BOSTON MEDICAL CENTER · PI SKOLNIK, PAUL R · 2002 to 2006
$1.1M
NCI NIH HHS CA68262NCI NIH HHS R01 CA068262NIAID NIH HHS 5T32 AI052070NIAID NIH HHS AI48082NIAID NIH HHS R01 AI048082NIAID NIH HHS T32 AI052070NIGMS NIH HHS GM47467NIGMS NIH HHS P01 GM047467
6 · The paper itself

Abstract

Encoded by a multigene family, ubiquitin is expressed in the form of three precursor proteins, two of which are fusions to the ribosomal subunits S27a and L40. Ubiquitin assists in ribosome biogenesis and also functions as a post-translational modifier after its release from S27a or L40. However, several species do not conserve the ribosomal ubiquitin domains. We report here the solution structure of a distant variant of ubiquitin, found at the N-terminus of S27a in Giardia lamblia, referred to as GlUb(S27a). Despite the considerable evolutionary distance that separates ubiquitin from GlUb(S27a), the structure of GlUb(S27a) is largely identical to that of ubiquitin. The variant domain remains attached to S27a and is part of the assembled holoribosome. Thus, conservation of tertiary structure suggests a role of this variant as a chaperone, while conservation of the primary structure--necessary for ubiquitin's function as a post-translational modifier--is no longer required. Based on these observations, we propose a model to explain the origin of the widespread ubiquitin superfold in eukaryotes.

Indexed as

Evolution, MolecularAmino Acid SequenceAnimalsGiardia lambliaHumansMass SpectrometryModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularPeptide HydrolasesProtein FoldingProtein Structure, SecondaryRibosomal ProteinsSequence AlignmentUbiquitinPeptide HydrolasesRibosomal Proteinsribosomal protein S27aUbiquitin

Identifiers

PMID17599068
PMCPMC1933403
OpenAlexW2013999462

What OpenQuestion holds

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Registered trials

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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.