Evidence map›Paper›PMID 12905021›Full record

ArticlePlanta2003

Subcellular localization of two types of ferrochelatase in cucumber.

T Masuda, T Suzuki, H Shimada, H Ohta, K Takamiya

Abstract read
PubMed Publisher
In one paragraph

Article in Planta, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
0.8field-weighted citation impact, top 31% 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

28 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Localization of heme biosynthesis in the diatomFrontiers in plant science · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Anatomic features, tolerance index, secondary metabolites and protein content of chickpea (Physiology and molecular biology of plants : an international journal of functional plant biology · 2020
    Article
  11. Proteomic analysis of haem-binding protein fromPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020
    Article
  12. Overexpression of chloroplast-targeted ferrochelatase 1 results in aPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020
    Article
  13. Article
  14. Plant Frataxin in Metal Metabolism.Frontiers in plant science · 2018
    Article
  15. Article
  16. Article
  17. Review
  18. Tetrapyrrole-based drought stress signalling.Plant biotechnology journal · 2015
    Review
  19. 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

5 authors at 1 institution in 1 country.

T MasudaGraduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, 226-8501 Yokohama, Japan. tmasuda@bio.titech.ac.jp
T Suzuki
H Shimada
H Ohta
K Takamiya
Tokyo Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

It is widely believed that ferrochelatase (protoheme ferrolyase, EC 4.99.1.1), which catalyzes the insertion of ferrous ion into protoporphyrin IX to form protoheme, exists in both plastids and mitochondria of higher plants. By in vitro import assay with isolated pea (Pisum sativum L.) organelles, it has been proposed that one of two isoforms of ferrochelatase (type 1) is dual-targeted into both plastids and mitochondria, and functions for heme biosynthesis in the both organelles. Recently, however, mitochondrial targeting of ferrochelatase is being disputed since pea mitochondria appeared to accept a variety of chloroplast proteins including the type-1 ferrochelatase of Arabidopsis thaliana (L.) Heynh. To clarify the precise subcellular localization of ferrochelatase in higher plants, here we investigated the subcellular localization of two types of ferrochelatase (CsFeC1 and CsFeC2) in cucumber (Cucumis sativus L.). In cotyledons, a significant level of specific ferrochelatase activity was detected in thylakoid membranes, but only a trace level of activity was detectable in mitochondria. Western blot analysis with specific antibodies showed that anti-CsFeC2 antiserum cross-reacted with plastids in photosynthetic and non-photosynthetic tissues. Anti-CsFeC1 did not cross-react with mitochondria, but CsFeC1 was clearly detectable in plastids from non-photosynthetic tissues. In situ transient-expression assays using green fluorescent protein demonstrated that, as well as CsFeC2, the N-terminal transit peptide of CsFeC1 targeted the fusion protein solely into plastids, but not into mitochondria. These results demonstrated that in cucumber both CsFeC1 and CsFeC2 are solely targeted into plastids, but not into mitochondria. Screening of a cucumber genomic or cDNA library did not allow any other ferrochelatase homologous gene to be isolated. The data presented here imply the reconsideration of mitochondrial heme biosynthesis in higher plants.

Indexed as

ChloroplastsCucumis sativusFerrochelataseGreen Fluorescent ProteinsImmunohistochemistryIsoenzymesLuminescent ProteinsMicroscopy, FluorescenceMitochondriaPhotosynthesisRecombinant Fusion ProteinsFerrochelataseGreen Fluorescent ProteinsIsoenzymesLuminescent ProteinsRecombinant Fusion Proteins

Identifiers

PMID12905021
OpenAlexW1972677973

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.