Evidence map›Paper›PMID 16980539›Full record

ArticleThe Plant cell2006

Structural and functional insights into the chloroplast ATP-dependent Clp protease in Arabidopsis.

Lars L E Sjögren, Tara M Stanne, Bo Zheng, Sirkka Sutinen, Adrian K Clarke

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

61 citing papers in PubMed, 133 citations in OpenAlex.

  1. Article
  2. Rapid COThe Plant journal : for cell and molecular biology · 2026
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  4. Northern Norway Sporophytes ofEcology and evolution · 2025
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  7. Role of cold shock proteins B and D inInfection and immunity · 2024
    Article
  8. Article
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  10. Article
  11. Review
  12. Computational and structural biotechnology journal · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Structural basis for the N-degron specificity of ClpS1 from Arabidopsis thaliana.Protein science : a publication of the Protein Society · 2021
    Article

1 more citing papers are in PubMed but not listed here.

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

5 authors at 2 institutions in 1 country.

Lars L E SjögrenDepartment of Plant and Environmental Sciences, Gothenburg University, 405 30 Gothenburg, Sweden.
Tara M Stanne
Bo Zheng
Sirkka Sutinen
Adrian K Clarke
University of Gothenburg · SEUmeå Plant Science Centre · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In contrast with the model Escherichia coli Clp protease, the ATP-dependent Clp protease in higher plants has a remarkably diverse proteolytic core consisting of multiple ClpP and ClpR paralogs, presumably arranged within a dual heptameric ring structure. Using antisense lines for the nucleus-encoded ClpP subunit, ClpP6, we show that the Arabidopsis thaliana Clp protease is vital for chloroplast development and function. Repression of ClpP6 produced a proportional decrease in the Clp proteolytic core, causing a chlorotic phenotype in young leaves that lessened upon maturity. Structural analysis of the proteolytic core revealed two distinct subcomplexes that likely correspond to single heptameric rings, one containing the ClpP1 and ClpR1-4 proteins, the other containing ClpP3-6. Proteomic analysis revealed several stromal proteins more abundant in clpP6 antisense lines, suggesting that some are substrates for the Clp protease. A proteolytic assay developed for intact chloroplasts identified potential substrates for the stromal Clp protease in higher plants, most of which were more abundant in young Arabidopsis leaves, consistent with the severity of the chlorotic phenotype observed in the clpP6 antisense lines. The identified substrates all function in more general housekeeping roles such as plastid protein synthesis, folding, and quality control, rather than in metabolic activities such as photosynthesis.

Indexed as

Adenosine TriphosphateArabidopsisChloroplastsElectrophoresis, Gel, Two-DimensionalEndopeptidase ClpMicroscopy, ElectronPhotosynthesisPlant LeavesProtein ConformationSubstrate SpecificityAdenosine TriphosphateEndopeptidase Clp

Identifiers

PMID16980539
PMCPMC1626633
OpenAlexW2114449891

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.