Evidence map›Paper›PMID 17369368›Full record

ArticleThe Plant cell2007

Chlorophyllase is a rate-limiting enzyme in chlorophyll catabolism and is posttranslationally regulated.

Smadar Harpaz-Saad, Tamar Azoulay, Tzahi Arazi, Eran Ben-Yaakov, Anahit Mett, Yoel M Shiboleth, Stefan Hörtensteiner, David Gidoni, Amit Gal-On, Eliezer E Goldschmidt and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

69 citing papers in PubMed, 247 citations in OpenAlex.

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  13. Genetic Architecture of Salt Tolerance in Cowpea (International journal of molecular sciences · 2023
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  17. Genes · 2023
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  18. Effect of exogenous melatonin on improvement of chlorophyll content and photochemical efficiency of PSII in mallow plants (Physiology and molecular biology of plants : an international journal of functional plant biology · 2023
    Article
  19. Article
  20. Article

9 more citing papers are in PubMed but not listed here.

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

11 authors at 3 institutions in 2 countries.

Smadar Harpaz-SaadInstitute of Plant Sciences, The Volcani Center, Agricultural Research Organization, Bet-Dagan 50250, Israel.
Tamar Azoulay
Tzahi Arazi
Eran Ben-Yaakov
Anahit Mett
Yoel M Shiboleth
Stefan Hörtensteiner
David Gidoni
Amit Gal-On
Eliezer E Goldschmidt
Yoram Eyal
Agricultural Research Organization · ILHebrew University of Jerusalem · ILUniversity of Bern · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chlorophyll is a central player in harvesting light energy for photosynthesis, yet the rate-limiting steps of chlorophyll catabolism and the regulation of the catabolic enzymes remain unresolved. To study the role and regulation of chlorophyllase (Chlase), the first enzyme of the chlorophyll catabolic pathway, we expressed precursor and mature versions of citrus (Citrus sinensis) Chlase in two heterologous plant systems: (1) squash (Cucurbita pepo) plants using a viral vector expression system; and (2) transiently transformed tobacco (Nicotiana tabacum) protoplasts. Expression of full-length citrus Chlase resulted in limited chlorophyll breakdown in protoplasts and no visible leaf phenotype in whole plants, whereas expression of a Chlase version lacking the N-terminal 21 amino acids (ChlaseDeltaN), which corresponds to the mature protein, led to extensive chlorophyll breakdown in both tobacco protoplasts and squash leaves. ChlaseDeltaN-expressing squash leaves displayed a dramatic chlorotic phenotype in plants grown under low-intensity light, whereas under natural light a lesion-mimic phenotype occurred, which was demonstrated to follow the accumulation of chlorophyllide, a photodynamic chlorophyll breakdown product. Full-length and mature citrus Chlase versions were localized to the chloroplast membrane fraction in expressing tobacco protoplasts, where processing of the N-terminal 21 amino acids appears to occur. Results obtained in both plant systems suggest that Chlase functions as a rate-limiting enzyme in chlorophyll catabolism controlled via posttranslational regulation.

Indexed as

Gene Expression Regulation, PlantCarboxylic Ester HydrolasesChlorophyllCitrus sinensisCucurbitaGene ExpressionGene Expression Regulation, EnzymologicGenetic VectorsIntracellular MembranesLightMutant ProteinsNicotianaPhenotypePlants, Genetically ModifiedProtoplastsRecombinant ProteinsCarboxylic Ester HydrolasesChlorophyllchlorophyllaseMutant ProteinsRecombinant ProteinsSerine

Identifiers

PMID17369368
PMCPMC1867358
OpenAlexW2128045412

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.