Evidence map›Paper›PMID 17592111›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

Dual specificities of the glyoxysomal/peroxisomal processing protease Deg15 in higher plants.

Michael Helm, Carsten Lück, Jakob Prestele, Georg Hierl, Pitter F Huesgen, Thomas Fröhlich, Georg J Arnold, Iwona Adamska, Angelika Görg, Friedrich Lottspeich and 1 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

54 citing papers in PubMed, 94 citations in OpenAlex.

  1. Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Translating theFrontiers in cell and developmental biology · 2022
    Review
  8. Anaerobic peroxisomes inProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Article
  10. Article
  11. APlant direct · 2019
    Article
  12. AProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. E3 ubiquitin ligase SP1 regulates peroxisome biogenesis in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  19. Article
  20. 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

11 authors at 5 institutions in 2 countries.

Michael HelmLehrstuhl für Botanik, Technische Universität München, Wissenschaftszentrum Weihenstephan, D-85350 Freising, Germany.
Carsten Lück
Jakob Prestele
Georg Hierl
Pitter F Huesgen
Thomas Fröhlich
Georg J Arnold
Iwona Adamska
Angelika Görg
Friedrich Lottspeich
Christine Gietl
Ludwig-Maximilians-Universität München · DEUniversity of Konstanz · DEMax Planck Institute of Biochemistry · DETechnical University of Munich · DEWashington State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glyoxysomes are a subclass of peroxisomes involved in lipid mobilization. Two distinct peroxisomal targeting signals (PTSs), the C-terminal PTS1 and the N-terminal PTS2, are defined. Processing of the PTS2 on protein import is conserved in higher eukaryotes. The cleavage site typically contains a Cys at P1 or P2. We purified the glyoxysomal processing protease (GPP) from the fat-storing cotyledons of watermelon (Citrullus vulgaris) by column chromatography, preparative native isoelectric focusing, and 2D PAGE. The GPP appears in two forms, a 72-kDa monomer and a 144-kDa dimer, which are in equilibrium with one another. The equilibrium is shifted on Ca(2+) removal toward the monomer and on Ca(2+) addition toward the dimer. The monomer is a general degrading protease and is activated by denatured proteins. The dimer constitutes the processing protease because the substrate specificity proven for the monomer (Phi-Arg/Lys downward arrow) is different from the processing substrate specificity (Cys-Xxx downward arrow/Xxx-Cys downward arrow) found with the mixture of monomer and dimer. The Arabidopsis genome analysis disclosed three proteases predicted to be in peroxisomes, a Deg-protease, a pitrilysin-like metallopeptidase, and a Lon-protease. Specific antibodies against the peroxisomal Deg-protease from Arabidopsis (Deg15) identify the watermelon GPP as a Deg15. A knockout mutation in the DEG15 gene of Arabidopsis (At1g28320) prevents processing of the glyoxysomal malate dehydrogenase precursor to the mature form. Thus, the GPP/Deg15 belongs to a group of trypsin-like serine proteases with Escherichia coli DegP as a prototype. Nevertheless, the GPP/Deg15 possesses specific characteristics and is therefore a new subgroup within the Deg proteases.

Indexed as

Protein Processing, Post-TranslationalArabidopsisArabidopsis ProteinsCitrullusEnzyme PrecursorsGlyoxysomesHeat-Shock ProteinsMalate DehydrogenaseMutationPeriplasmic ProteinsPeroxisomesPlant ProteinsPlants, Genetically ModifiedSerine EndopeptidasesSubstrate SpecificityArabidopsis ProteinsDeg15 protein, ArabidopsisDegP proteaseEnzyme PrecursorsHeat-Shock ProteinsMalate DehydrogenasePeriplasmic ProteinsPlant ProteinsSerine Endopeptidases

Identifiers

PMID17592111
PMCPMC2040927
OpenAlexW1969867336

What OpenQuestion holds

Textmetadata
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.