Evidence map›Paper›PMID 30463523›Full record

ArticleBMC plant biology2018

Proteomic analysis of the response of Funnelifor mismosseae/Medicago sativa to atrazine stress.

Xin Sui, Qi Wu, Wei Chang, Xiaoxu Fan, Fuqiang Song

Abstract 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 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

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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

5 authors.

Xin SuiHeilongjiang Provincial Key Laboratory of Ecologial Restoration and Resource Utilization for Cold Region, School of Life Sciences, Heilongjiang University, XueFu Road No.74, Nangang district, Harbin City, 150080, People's Republic of China.ORCID http://orcid.org/0000-0002-4339-4308
Qi WuHeilongjiang Provincial Key Laboratory of Ecologial Restoration and Resource Utilization for Cold Region, School of Life Sciences, Heilongjiang University, XueFu Road No.74, Nangang district, Harbin City, 150080, People's Republic of China.
Wei ChangHeilongjiang Provincial Key Laboratory of Ecologial Restoration and Resource Utilization for Cold Region, School of Life Sciences, Heilongjiang University, XueFu Road No.74, Nangang district, Harbin City, 150080, People's Republic of China.
Xiaoxu FanHeilongjiang Provincial Key Laboratory of Ecologial Restoration and Resource Utilization for Cold Region, School of Life Sciences, Heilongjiang University, XueFu Road No.74, Nangang district, Harbin City, 150080, People's Republic of China.
Fuqiang SongHeilongjiang Provincial Key Laboratory of Ecologial Restoration and Resource Utilization for Cold Region, School of Life Sciences, Heilongjiang University, XueFu Road No.74, Nangang district, Harbin City, 150080, People's Republic of China. 0431sfq@163.com.

Funding

National Natural Science Foundation of China 31270535National Natural Science Foundation of China 31500431National Natural Science Foundation of China 31570635Outstanding Youth Science Foundation of Heilongjiang Province JC201306
6 · The paper itself

Abstract

backgroundArbuscular mycorrhizal (AM) fungi form symbiotic associations with host plants can protect host plants against diverse biotic and abiotic stresses, and promote biodegradation of various contaminants. However, the molecular mechanisms of how the arbuscular mycorrhizal fungi and host plant association on atrazine stress were still poorly understood. To better characterize how arbuscular mycorrhizal fungi and host plant interactions increase atrazine stress, we performed physiological and proteomic analysis of Funneliformis mosseae (mycorrhizal fungi) and Medicago sativa (alfalfa) association under atrazine stress.

resultsThe results showed that in the Arbuscular mycorrhizal, protective enzymes were up regulated and the malondialdehyde content increased relative to those of non-mycorrhizal M.sativa. We also examined the atrazine degradation rates within the nutrient solution, and a 44.43% reduction was observed with the mycorrhizal M.sativa, with 30.83% of the reduction attributed to F. mosseae. The accumulation content in root and stem of mycorrhizal M.sativa were obviously increased 11.89% and 16.33% than those of non- mycorrhizal M.sativa. The activity of PPO, POD, CAT and SOD in mycorrhizal M.sativa were obviously higher than non mycorrhizal M.sativa under atrazine stess. We identified differential root proteins using isobaric tags for relative and absolute quantization coupled with liquid chromatography-mass spectrometry, with 533 proteins identified (276 unregulated and 257 downregulated). The differentially expressed proteins were further examined using GO, BLAST comparisons, and a literature inquiry and were classified into the categories of atrazine degradation (37.1%); atrazine stress response (28.6%); plant immune responses (14.3%); translation, synthesis, and processing (10%); and signal transduction and biological processes (10%). Furthermore, we identified glycosyl transferase, glutathione S-transferase, laccase, cytochrome P450 monooxygenase, peroxidase, and other proteins closely related to the degradation process.

conclusionsMycorrhizal Medicago showed improved atrazine degradation within the culturing medium and increased atrazine enrichment in the roots and stems. Additionally, AMF increased the plant root response to atrazine, with relevant enzymes up regulated and toxic effects alleviated. Overall, the findings of this study show that AMF played an important role in easing atrazine stress in plants and contributed to atrazine remediation and further contributed to the understanding of the molecular mechanism associated with atrazine stresses and potential mycorrhizal contributions in M.sativa.

Indexed as

AtrazineBiodegradation, EnvironmentalGlomeromycotaHerbicidesMedicago sativaMycorrhizaePlant ProteinsProteomeSoil PollutantsSymbiosisAtrazineHerbicidesPlant ProteinsProteomeSoil PollutantsArbuscular mycorrhizaAtrazineMDAMedicago sativaProtective enzyme systemProteome

Identifiers

PMID30463523
PMCPMC6247736

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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.