Evidence map›Paper›PMID 22829322›Full record

ArticlePlant physiology2012

Photosynthetic adaptation to length of day is dependent on S-sulfocysteine synthase activity in the thylakoid lumen.

María Ángeles Bermúdez, Jeroni Galmés, Inmaculada Moreno, Philip M Mullineaux, Cecilia Gotor, Luis C Romero

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

22 citing papers in PubMed, 41 citations in OpenAlex.

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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

6 authors at 4 institutions in 1 country.

María Ángeles BermúdezInstituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas y Universidad de Sevilla, 41092 Seville, Spain.
Jeroni Galmés
Inmaculada Moreno
Philip M Mullineaux
Cecilia Gotor
Luis C Romero
Instituto de Bioquímica Vegetal y Fotosíntesis · ESConsejo Superior de Investigaciones Científicas · ESUniversidad de Sevilla · ESUniversitat de les Illes Balears · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arabidopsis (Arabidopsis thaliana) chloroplasts contain two O-acetyl-serine(thiol)lyase (OASTL) homologs, OAS-B, which is an authentic OASTL, and CS26, which has S-sulfocysteine synthase activity. In contrast with OAS-B, the loss of CS26 function resulted in dramatic phenotypic changes, which were dependent on the light treatment. We have performed a detailed characterization of the photosynthetic and chlorophyll fluorescence parameters in cs26 plants compared with those of wild-type plants under short-day growth conditions (SD) and long-day growth conditions (LD). Under LD, the photosynthetic characterization, which was based on substomatal CO(2) concentrations and CO(2) concentration in the chloroplast curves, revealed significant reductions in most of the photosynthetic parameters for cs26, which were unchanged under SD. These parameters included net CO(2) assimilation rate, mesophyll conductance, and mitochondrial respiration at darkness. The analysis also showed that cs26 under LD required more absorbed quanta per driven electron flux and fixed CO(2). The nonphotochemical quenching values suggested that in cs26 plants, the excess electrons that are not used in photochemical reactions may form reactive oxygen species. A photoinhibitory effect was confirmed by the background fluorescence signal values under LD and SD, which were higher in young leaves compared with mature ones under SD. To hypothesize the role of CS26 in relation to the photosynthetic machinery, we addressed its location inside of the chloroplast. The activity determination and localization analyses that were performed using immunoblotting indicated the presence of an active CS26 enzyme exclusively in the thylakoid lumen. This finding was reinforced by the observation of marked alterations in many lumenal proteins in the cs26 mutant compared with the wild type.

Indexed as

AcclimatizationPhotoperiodPhotosynthesisArabidopsisCarbon DioxideChlorophyllCysteine SynthaseElectrophoresis, Gel, Two-DimensionalEnzyme ActivationFluorescenceLightLyasesPhenotypePhotochemical ProcessesPlant LeavesProteomicsCarbon DioxideChlorophyllCysteine SynthaseLyasesReactive Oxygen SpeciesS-sulfocysteine synthase

Identifiers

PMID22829322
PMCPMC3440205
OpenAlexW2078877348

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.