Evidence map›Paper›PMID 23898032›Full record

ArticleThe Plant cell2013

ClpS1 is a conserved substrate selector for the chloroplast Clp protease system in Arabidopsis.

Kenji Nishimura, Yukari Asakura, Giulia Friso, Jitae Kim, Soo-Hyun Oh, Heidi Rutschow, Lalit Ponnala, Klaas J van Wijk

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

56 citing papers in PubMed, 125 citations in OpenAlex.

  1. Article
  2. Assessment of Bacterial N-Degron Proteolysis by a Dual-Fluorescence Reporter.Methods in molecular biology (Clifton, N.J.) · 2026
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  12. CRL2Nature communications · 2022
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  15. Article
  16. Review
  17. Structural basis for the N-degron specificity of ClpS1 from Arabidopsis thaliana.Protein science : a publication of the Protein Society · 2021
    Article
  18. Article
  19. Frontiers in plant science · 2021
    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

8 authors at 1 institution in 1 country.

Kenji NishimuraDepartment of Plant Biology, Cornell University, Ithaca, New York 14853, USA.
Yukari Asakura
Giulia Friso
Jitae Kim
Soo-Hyun Oh
Heidi Rutschow
Lalit Ponnala
Klaas J van Wijk
Cornell University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Whereas the plastid caseinolytic peptidase (Clp) P protease system is essential for plant development, substrates and substrate selection mechanisms are unknown. Bacterial ClpS is involved in N-degron substrate selection and delivery to the ClpAP protease. Through phylogenetic analysis, we show that all angiosperms contain ClpS1 and some species also contain ClpS1-like protein(s). In silico analysis suggests that ClpS1 is the functional homolog of bacterial ClpS. We show that Arabidopsis thaliana ClpS1 interacts with plastid ClpC1,2 chaperones. The Arabidopsis ClpS1 null mutant (clps1) lacks a visible phenotype, and no genetic interactions with ClpC/D chaperone or ClpPR core mutants were observed. However, clps1, but not clpc1-1, has increased sensitivity to the translational elongation inhibitor chloramphenicol suggesting a link between translational capacity and ClpS1. Moreover, ClpS1 was upregulated in clpc1-1, and quantitative proteomics of clps1, clpc1, and clps1 clpc1 showed specific molecular phenotypes attributed to loss of ClpC1 or ClpS1. In particular, clps1 showed alteration of the tetrapyrrole pathway. Affinity purification identified eight candidate ClpS1 substrates, including plastid DNA repair proteins and Glu tRNA reductase, which is a control point for tetrapyrrole synthesis. ClpS1 interaction with five substrates strictly depended on two conserved ClpS1 residues involved in N-degron recognition. ClpS1 function, substrates, and substrate recognition mechanisms are discussed.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsBlotting, WesternChloroplastsElectrophoresis, Polyacrylamide GelEndopeptidase ClpIsoenzymesModels, GeneticMolecular ChaperonesMolecular Sequence DataMutationPhylogenyPlants, Genetically ModifiedProtein BindingProtein Interaction MappingArabidopsis ProteinsEndopeptidase ClpIsoenzymesMolecular Chaperones

Identifiers

PMID23898032
PMCPMC3723626
OpenAlexW2108284180

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.