Evidence map›Paper›PMID 18192382›Full record

ArticleJournal of bacteriology2008

The C-terminal extension of ferrochelatase is critical for enzyme activity and for functioning of the tetrapyrrole pathway in Synechocystis strain PCC 6803.

Roman Sobotka, Samantha McLean, Monika Zuberova, C Neil Hunter, Martin Tichy

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

24 citing papers in PubMed, 42 citations in OpenAlex.

  1. Epigenetic control of tetrapyrrole biosynthesis by m4C DNA methylation in a cyanobacterium.DNA research : an international journal for rapid publication of reports on genes and genomes · 2024
    Article
  2. Article
  3. Article
  4. Biosynthesis of the modified tetrapyrroles-the pigments of life.The Journal of biological chemistry · 2020
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.Microbiology and molecular biology reviews : MMBR · 2017
    Review
  10. The Complex Transcriptional Response ofG3 (Bethesda, Md.) · 2017
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
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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 3 institutions in 2 countries.

Roman SobotkaInstitute of Microbiology, Department of Autotrophic Microorganisms, Opatovicky mlyn, 379 81 Trebon, Czech Republic. sobotka@alga.cz
Samantha McLean
Monika Zuberova
C Neil Hunter
Martin Tichy
University of Sheffield · GBUniversity of South Bohemia in České Budějovice · CZCzech Academy of Sciences, Institute of Microbiology · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heme and chlorophyll (Chl) share a common biosynthetic pathway up to the branch point where magnesium chelatase and ferrochelatase (FeCH) insert either magnesium for Chl biosynthesis or ferrous iron for heme biosynthesis. A distinctive feature of FeCHs in cyanobacteria is their C-terminal extension, which forms a putative transmembrane segment containing a Chl-binding motif. We analyzed the deltaH324 strain of Synechocystis sp. strain PCC 6803, which contains a truncated FeCH enzyme lacking this C-terminal domain. Truncated FeCH was localized to the membrane fraction, suggesting that the C-terminal domain is not necessary for membrane association of the enzyme. Measurements of enzyme activity and complementation experiments revealed that the deltaH324 mutation dramatically reduced activity of the FeCH, which resulted in highly upregulated 5-aminolevulinic acid synthesis in the deltaH324 mutant, implying a direct role for heme in the regulation of flux through the pathway. Moreover, the deltaH324 mutant accumulated a large amount of protoporphyrin IX, and levels of Chl precursors were also significantly increased, suggesting that some, but not all, of the "extra" flux can be diverted down the Chl branch. Analysis of the recombinant full-length and truncated FeCHs demonstrated that the C-terminal extension is critical for activity of the FeCH and that it is strictly required for oligomerization of this enzyme. The observed changes in tetrapyrrole trafficking and the role of the C terminus in the functioning of FeCH are discussed.

Indexed as

Aminolevulinic AcidBacterial ProteinsBlotting, WesternFerrochelataseImmunoblottingModels, BiologicalMutationProtoporphyrinsRecombinant ProteinsSynechocystisTetrapyrrolesAminolevulinic AcidBacterial ProteinsFerrochelataseprotoporphyrin IXProtoporphyrinsRecombinant ProteinsTetrapyrroles

Identifiers

PMID18192382
PMCPMC2258870
OpenAlexW2170728112

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.