Evidence map›Paper›PMID 14688293›Full record

ArticleThe Plant cell2004

Storage protein accumulation in the absence of the vacuolar processing enzyme family of cysteine proteases.

Darren Gruis, Jan Schulze, Rudolf Jung

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
13.2field-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

55 citing papers in PubMed, 160 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Plant cathepsin B, a versatile protease.Frontiers in plant science · 2024
    Review
  5. The putative vacuolar processing enzyme gene TaVPE3cB is a candidate gene for wheat stem pith-thickness.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2023
    Article
  6. Article
  7. Article
  8. Post-translational cleavage of HMW-GSMolecular breeding : new strategies in plant improvement · 2021
    Article
  9. Review
  10. Article
  11. Article
  12. Structural and functional studies ofThe Journal of biological chemistry · 2020
    Article
  13. Article
  14. Article
  15. Plant Vacuolar Processing Enzymes.Frontiers in plant science · 2019
    Review
  16. Article
  17. Article
  18. 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

3 authors at 1 institution in 1 country.

Darren GruisPioneer Hi-Bred International, A DuPont Company, Johnston, Iowa 50131-1004, USA.
Jan Schulze
Rudolf Jung
Pioneer Hi-Bred · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The role(s) of specific proteases in seed protein processing is only vaguely understood; indeed, the overall role of processing in stable protein deposition has been the subject of more speculation than direct investigation. Seed-type members of the vacuolar processing enzyme (VPE) family were hypothesized to perform a unique function in seed protein processing, but we demonstrated previously that Asn-specific protein processing in developing Arabidopsis seeds occurs independently of this VPE activity. Here, we describe the unexpected expression of vegetative-type VPEs in developing seeds and test the role(s) of all VPEs in seed storage protein accumulation by systematically stacking knockout mutant alleles of all four members (alphaVPE, betaVPE, gammaVPE, and deltaVPE) of the VPE gene family in Arabidopsis. The complete removal of VPE function in the alphavpe betavpe gammavpe deltavpe quadruple mutant resulted in a total shift of storage protein accumulation from wild-type processed polypeptides to a finite number of prominent alternatively processed polypeptides cleaved at sites other than the conserved Asn residues targeted by VPE. Although alternatively proteolyzed legumin-type globulin polypeptides largely accumulated as intrasubunit disulfide-linked polypeptides with apparent molecular masses similar to those of VPE-processed legumin polypeptides, they showed markedly altered solubility and protein assembly characteristics. Instead of forming 11S hexamers, alternatively processed legumin polypeptides were deposited primarily as 9S complexes. However, despite the impact on seed protein processing, plants devoid of all known functional VPE genes appeared unchanged with regard to protein content in mature seeds, relative mobilization rates of protein reserves during germination, and vegetative growth. These findings indicate that VPE-mediated Asn-specific proteolytic processing, and the physiochemical property changes attributed to this specific processing step, are not required for the successful deposition and mobilization of seed storage protein in the protein storage vacuoles of Arabidopsis seeds.

Indexed as

AllelesAmino Acid SequenceArabidopsisArabidopsis ProteinsCysteine EndopeptidasesElectrophoresis, Polyacrylamide GelGene Expression Regulation, EnzymologicGene Expression Regulation, PlantGerminationGlobulinsLeguminsMolecular Sequence DataMutationPlant ProteinsSeedsArabidopsis ProteinsCysteine EndopeptidasesGlobulinsLeguminsPlant Proteinsvacuolar processing enzyme

Identifiers

PMID14688293
PMCPMC301410
OpenAlexW2106190285

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.