Evidence map›Paper›PMID 26172838›Full record

ArticlePloS one2015

Lil3 Assembles with Proteins Regulating Chlorophyll Synthesis in Barley.

Astrid Mork-Jansson, Ann Kristin Bue, Daniela Gargano, Clemens Furnes, Veronika Reisinger, Janine Arnold, Karol Kmiec, Lutz Andreas Eichacker

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

13 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. LHC-like Proteins: The Guardians of Photosynthesis.International journal of molecular sciences · 2023
    Review
  3. Review
  4. Genome-wide association identifies a missing hydrolase for tocopherol synthesis in plants.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Review
  6. Article
  7. Review
  8. 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

8 authors at 1 institution in 1 country.

Astrid Mork-JanssonCenter for Organelle Research, University of Stavanger, Stavanger, Norway.
Ann Kristin BueCenter for Organelle Research, University of Stavanger, Stavanger, Norway.
Daniela GarganoCenter for Organelle Research, University of Stavanger, Stavanger, Norway.
Clemens FurnesCenter for Organelle Research, University of Stavanger, Stavanger, Norway.
Veronika ReisingerCenter for Organelle Research, University of Stavanger, Stavanger, Norway.
Janine ArnoldCenter for Organelle Research, University of Stavanger, Stavanger, Norway.
Karol KmiecCenter for Organelle Research, University of Stavanger, Stavanger, Norway.
Lutz Andreas EichackerCenter for Organelle Research, University of Stavanger, Stavanger, Norway.
University of Stavanger · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The light-harvesting-like (LIL) proteins are a family of membrane proteins that share a chlorophyll a/b-binding motif with the major light-harvesting antenna proteins of oxygenic photoautotrophs. LIL proteins have been associated with the regulation of tetrapyrrol biosynthesis, and plant responses to light-stress. Here, it was found in a native PAGE approach that chlorophyllide, and chlorophyllide plus geranylgeraniolpyrophosphate trigger assembly of Lil3 in three chlorine binding fluorescent protein bands, termed F1, F2, and F3. It is shown that light and chlorophyllide trigger accumulation of protochlorophyllide-oxidoreductase, and chlorophyll synthase in band F3. Chlorophyllide and chlorophyll esterified to geranylgeraniol were identified as basis of fluorescence recorded from band F3. A direct interaction between Lil3, CHS and POR was confirmed in a split ubiquitin assay. In the presence of light or chlorophyllide, geranylgeraniolpyrophosphate was shown to trigger a loss of the F3 band and accumulation of Lil3 and geranylgeranyl reductase in F1 and F2. No direct interaction between Lil3 and geranylgeraniolreductase was identified in a split ubiquitin assay; however, accumulation of chlorophyll esterified to phytol in F1 and F2 corroborated the enzymes assembly. Chlorophyll esterified to phytol and the reaction center protein psbD of photosystem II were identified to accumulate together with psb29, and APX in the fluorescent band F2. Data show that Lil3 assembles with proteins regulating chlorophyll synthesis in etioplasts from barley (Hordeum vulgare L.).

Indexed as

ChlorophyllChlorophyll AChloroplastsHordeumLightLight-Harvesting Protein ComplexesOxidoreductasesPhotosystem II Protein ComplexPhytolProtein BindingChlorophyllChlorophyll Achlorophyll bgeranylgeranyl reductaseLight-Harvesting Protein ComplexesOxidoreductasesPhotosystem II Protein ComplexPhytol

Identifiers

PMID26172838
PMCPMC4501709
OpenAlexW1571890855

What OpenQuestion holds

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LicenceCC BY
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.