Evidence map›Paper›PMID 15159633›Full record

ArticlePlant molecular biology2004

A small family of LLS1-related non-heme oxygenases in plants with an origin amongst oxygenic photosynthesizers.

John Gray, Ellen Wardzala, Manli Yang, Steffen Reinbothe, Steve Haller, Florencia Pauli

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Plant molecular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

34 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Article
  3. Evolution of chlorophyll degradation is associated with plant transition to land.The Plant journal : for cell and molecular biology · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. A Protochlorophyllide (Pchlide)Frontiers in plant science · 2019
    Article
  10. Article
  11. Article
  12. Article
  13. Roles and maturation of iron-sulfur proteins in plastids.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Phylogenetic analysis reveals the surprising diversity of an oxygenase class.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012
    Article
  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

6 authors at 3 institutions in 2 countries.

John GrayDepartment of Biological Sciences, University of Toledo, 2801 West Bancroft Street, Toledo, OH 43606, USA. jgray5@uoft02.utoledo.edu
Ellen Wardzala
Manli Yang
Steffen Reinbothe
Steve Haller
Florencia Pauli
University of Toledo · USStanford University · USUniversité Joseph Fourier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Conservation of Lethal-leaf spot 1 (Lls1) lesion mimic gene in land plants including moss is consistent with its recently reported function as pheophorbide a oxygenase (Pao) which catalyzes a key step in chlorophyll degradation (Pruzinska et al., 2003). A bioinformatics survey of complete plant genomes reveals that LLS1(PAO) belongs to a small 5-member family of non-heme oxygenases defined by the presence of Rieske and mononuclear iron-binding domains. This gene family includes chlorophyll a oxygenase (Cao), choline monooxygenase (Cmo), the gene for a 55 kDa protein associated with protein transport through the inner chloroplast membrane (Tic 55) and a novel 52 kDa protein isolated from chloroplasts (Ptc 52). Analysis of gene structure reveals that these genes diverged prior to monocot/dicot divergence. Homologues of LLS1(PAO), CAO, TIC55 and PTC52 but not CMO are found in the genomes of several cyanobacteria. LLS1(PAO), PTC52, TIC55 and a set of related cyanobacterial homologues share an extended carboxyl terminus containing a novel F/Y/W-x(2)-H-x(3)-C-x(2)-C motif not present in CAO. These proteins appear to have evolved during the transition to oxygenic photosynthesis to play various roles in chlorophyll metabolism. In contrast, CMO homologues are found only in plants and are most closely related to aromatic ring-hydroxylating enzymes from soil-dwelling bacteria, suggesting a more recent evolution of this enzyme, possibly by horizontal gene transfer. Our phylogenetic analysis of 95 extant non-heme dioxygenases provides a useful framework for the classification of LLS1(PAO)-related non-heme oxygenases.

Indexed as

Evolution, MolecularAmino Acid MotifsAmino Acid SequenceApoptosis Regulatory ProteinsArabidopsisArabidopsis ProteinsBacteriaConserved SequenceCyanobacteriaGenes, PlantIron-Binding ProteinsMolecular Sequence DataOxygenOxygenasesPhotosynthesisPhylogenyACD1 protein, ArabidopsisApoptosis Regulatory ProteinsArabidopsis ProteinsIron-Binding ProteinsOxygenOxygenases

Identifiers

PMID15159633
OpenAlexW1993679462

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.