Evidence map›Paper›PMID 29320985›Full record

ArticleBMC plant biology2018

Chlorophyll fluorescence analysis revealed essential roles of FtsH11 protease in regulation of the adaptive responses of photosynthetic systems to high temperature.

Junping Chen, John J Burke, Zhanguo Xin

Open access · goldAbstract read
In one paragraph

Article in BMC plant biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

28 citing papers in PubMed, 73 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

3 authors at 1 institution in 1 country.

Junping ChenPlant Stress and Germplasm Development Unit, USDA-ARS, 3810 4th Street, Lubbock, TX, 79415, USA. junping.chen@ars.usda.gov.ORCID 0000-0001-9060-8017
John J BurkePlant Stress and Germplasm Development Unit, USDA-ARS, 3810 4th Street, Lubbock, TX, 79415, USA.
Zhanguo XinPlant Stress and Germplasm Development Unit, USDA-ARS, 3810 4th Street, Lubbock, TX, 79415, USA.
Agricultural Research Service · US

Funding

United States - Israel Binational Agricultural Research and Development Fund US-422-09
6 · The paper itself

Abstract

backgroundPhotosynthetic systems are known to be sensitive to high temperature stress. To maintain a relatively "normal" level of photosynthetic activities, plants employ a variety of adaptive mechanisms in response to environmental temperature fluctuations. Previously, we reported that the chloroplast-targeted AtFtsH11 protease played an essential role for Arabidopsis plants to survive at high temperatures and to maintain normal photosynthetic efficiency at moderately elevated temperature. To investigate the factors contributing to the photosynthetic changes in FtsH11 mutant, we performed detailed chlorophyll fluorescence analyses of dark-adapted mutant plants and compared them to Col-0 WT plants under normal, two moderate high temperatures, and a high light conditions.

resultsWe found that mutation of FtsH11 gene caused significant decreases in photosynthetic efficiency of photosystems when environmental temperature raised above optimal. Under moderately high temperatures, the FtsH11 mutant showed significant 1) decreases in electron transfer rates of photosystem II (PSII) and photosystem I (PSI), 2) decreases in photosynthetic capabilities of PSII and PSI, 3) increases in non-photochemical quenching, and a host of other chlorophyll fluorescence parameter changes. We also found that the degrees of these negative changes for utilizing the absorbed light energy for photosynthesis in FtsH11 mutant were correlated with the level and duration of the heat treatments. For plants grown under normal temperature and subjected to the high light treatment, no significant difference in chlorophyll fluorescence parameters was found between the FtsH11 mutant and Col-0 WT plants.

conclusionsThe results of this study show that AtFtsH11 is essential for normal photosynthetic function under moderately elevated temperatures. The results also suggest that the network mediated by AtFtsH11 protease plays critical roles for maintaining the thermostability and possibly structural integrity of both photosystems under elevated temperatures. Elucidating the underlying mechanisms of FtsH11 protease in photosystems may lead to improvement of photosynthetic efficiency under heat stress conditions, hence, plant productivity.

Indexed as

Hot TemperatureLightArabidopsisArabidopsis ProteinsChlorophyllFluorescenceMetalloproteasesMutationPhotosynthesisArabidopsis ProteinsChlorophyllFtsH11 protein, ArabidopsisMetalloproteasesChlorophyll fluorescenceFtsH11Heat stressHigh temperaturePhotosynthesis; ThermostabilityThermotolerance

Identifiers

PMID29320985
PMCPMC5763919
OpenAlexW2783616733

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Registered trials

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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.