Evidence map›Paper›PMID 26419670›Full record

ArticleThe Plant cell2015

Discovery of a Unique Clp Component, ClpF, in Chloroplasts: A Proposed Binary ClpF-ClpS1 Adaptor Complex Functions in Substrate Recognition and Delivery.

Kenji Nishimura, Janina Apitz, Giulia Friso, Jitae Kim, Lalit Ponnala, Bernhard Grimm, Klaas J van Wijk

Open access · hybridAbstract read
In one paragraph

Article in The Plant cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

42 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. A mutation in LacDWARF1 results in a GA-deficient dwarf phenotype in sponge gourd (Luffa acutangula).TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2021
    Article
  16. The FtsHi Enzymes ofInternational journal of molecular sciences · 2021
    Review
  17. Article
  18. Article
  19. Article
  20. Progression from remodeling to hibernation of ribosomes in zinc-starved mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Kenji NishimuraDepartment of Plant Biology, Cornell University, Ithaca, New York 14853.
Janina ApitzDepartment of Plant Physiology, Humboldt University, 10115 Berlin, Germany.
Giulia FrisoDepartment of Plant Biology, Cornell University, Ithaca, New York 14853.
Jitae KimDepartment of Plant Biology, Cornell University, Ithaca, New York 14853.
Lalit PonnalaComputational Biology Service Unit, Cornell University, Ithaca, New York 14853.
Bernhard GrimmDepartment of Plant Physiology, Humboldt University, 10115 Berlin, Germany.
Klaas J van WijkDepartment of Plant Biology, Cornell University, Ithaca, New York 14853 kv35@cornell.edu.ORCID http://orcid.org/0000-0001-9536-0487
Cornell University · USHumboldt-Universität zu Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Clp proteases are found in prokaryotes, mitochondria, and plastids where they play crucial roles in maintaining protein homeostasis (proteostasis). The plant plastid Clp machinery comprises a hetero-oligomeric ClpPRT proteolytic core, ATP-dependent chaperones ClpC and ClpD, and an adaptor protein, ClpS1. ClpS1 selects substrates to the ClpPR protease-ClpC chaperone complex for degradation, but the underlying substrate recognition and delivery mechanisms are currently unclear. Here, we characterize a ClpS1-interacting protein in Arabidopsis thaliana, ClpF, which can interact with the Clp substrate glutamyl-tRNA reductase. ClpF and ClpS1 mutually stimulate their association with ClpC. ClpF, which is only found in photosynthetic eukaryotes, contains bacterial uvrB/C and YccV protein domains and a unique N-terminal domain. We propose a testable model in which ClpS1 and ClpF form a binary adaptor for selective substrate recognition and delivery to ClpC, reflecting an evolutionary adaptation of the Clp system to the plastid proteome.

Indexed as

Models, MolecularProteomeAdaptor Proteins, Signal TransducingAldehyde OxidoreductasesArabidopsisArabidopsis ProteinsCarrier ProteinsChloroplastsEndopeptidase ClpMolecular ChaperonesMultienzyme ComplexesMutationPhylogenyProtein Interaction MappingSequence Analysis, DNASubstrate SpecificityAdaptor Proteins, Signal TransducingAldehyde OxidoreductasesArabidopsis ProteinsCarrier ProteinsClpF protein, ArabidopsisClpS1 protein, ArabidopsisEndopeptidase Clpglutamyl tRNA reductaseMolecular ChaperonesMultienzyme ComplexesProteome

Identifiers

PMID26419670
PMCPMC4682326
OpenAlexW2179109865

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.