Evidence map›Paper›PMID 28061816›Full record

ArticleBMC plant biology2017

Major Cys protease activities are not essential for senescence in individually darkened Arabidopsis leaves.

Adriana Pružinská, Takayuki Shindo, Sherry Niessen, Farnusch Kaschani, Réka Tóth, A Harvey Millar, Renier A L van der Hoorn

Open access · goldAbstract read
In one paragraph

Article in BMC plant biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

21 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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  5. Article
  6. Article
  7. Article
  8. Plant cathepsin B, a versatile protease.Frontiers in plant science · 2024
    Review
  9. Review
  10. Article
  11. Transient proteolysis reduction ofFrontiers in plant science · 2022
    Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. A New Role for SAG12 Cysteine Protease in Roots ofFrontiers in plant science · 2018
    Article
  20. Review
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

7 authors at 5 institutions in 4 countries.

Adriana PružinskáThe Plant Chemetics laboratory, Max Planck Institute for Plant Breeding Research, 50829, Cologne, Germany.
Takayuki ShindoThe Plant Chemetics laboratory, Max Planck Institute for Plant Breeding Research, 50829, Cologne, Germany.
Sherry NiessenThe Skaggs Institute for Chemical Biology and Department of Chemical Physiology, The Center for Physiological Proteomics, The Scripps Research Institute, La Jolla, 92037, California, USA.
Farnusch KaschaniThe Plant Chemetics laboratory, Max Planck Institute for Plant Breeding Research, 50829, Cologne, Germany.
Réka TóthDepartment of Plant Developmental Biology, Max Planck Institute for Plant Breeding Research, 50829, Cologne, Germany.
A Harvey MillarThe Australian Research Council Centre of Excellence in Plant Energy Biology, The University of Western Australia, Perth, WA, Australia.
Renier A L van der HoornThe Plant Chemetics laboratory, Max Planck Institute for Plant Breeding Research, 50829, Cologne, Germany. renier.vanderhoorn@plants.ox.ac.uk.
Max Planck Institute for Plant Breeding Research · DEARC Centre of Excellence in Plant Energy Biology · AUAustralian Research Council · AUScripps Research Institute · USUniversity of Oxford · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundPapain-like Cys Proteases (PLCPs) and Vacuolar Processing Enzymes (VPEs) are amongst the most highly expressed proteases during leaf senescence in Arabidopsis. Using activity-based protein profiling (ABPP), a method that enables detection of active enzymes within a complex sample using chemical probes, the activities of PLCPs and VPEs were investigated in individually darkened leaves of Arabidopsis, and their role in senescence was tested in null mutants.

resultsABPP and mass spectrometry revealed an increased activity of several PLCPs, particularly RD21A and AALP. By contrast, despite increased VPE transcript levels, active VPE decreased in individually darkened leaves. Eight protease knock-out lines and two protease over expressing lines were subjected to senescence phenotype analysis to determine the importance of individual protease activities to senescence. Unexpectedly, despite the absence of dominating PLCP activities in these plants, the rubisco and chlorophyll decline in individually darkened leaves and the onset of whole plant senescence were unaltered. However, a significant delay in progression of whole plant senescence was observed in aalp-1 and rd21A-1/aalp-1 mutants, visible in the reduced number of senescent leaves.

conclusionsMajor Cys protease activities are not essential for dark-induced and developmental senescence and only a knock out line lacking AALP shows a slight but significant delay in plant senescence.

Indexed as

ArabidopsisArabidopsis ProteinsChlorophyllCysteine ProteasesDarknessPlant LeavesRibulose-Bisphosphate CarboxylaseArabidopsis ProteinsChlorophyllCysteine ProteasesRibulose-Bisphosphate CarboxylaseActivity-based protein profilingPapain-like proteasesSenescenceVacuolar processing enzymes

Identifiers

PMID28061816
PMCPMC5217659
OpenAlexW2567793289

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.