Evidence map›Paper›PMID 36253724›Full record

ArticleBMC plant biology2022

Gene Identification, expression analysis and molecular docking of ATP sulfurylase in the selenization pathway of Cardamine hupingshanensis.

Zhijing Xiao, Yanke Lu, Yi Zou, Chi Zhang, Li Ding, Kai Luo, Qiaoyu Tang, Yifeng Zhou

Open access · goldAbstract read
In one paragraph

Article in BMC plant biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

8 citing papers in PubMed, 14 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

8 authors at 2 institutions in 1 country.

Zhijing XiaoHubei Key Laboratory of Biological Resources Protection and Utilization, Hubei Minzu University, 44500, Enshi, China.
Yanke LuCollege of Biological and Food Engineering, Hubei Minzu University, 44500, Enshi, China.
Yi ZouHubei Minzu University Affiliated Enshi Clinical Medical School, The Central Hospital of Enshi Tujia and Miao Autonomous Prefecture, 445000, Enshi, Hubei, China.
Chi ZhangCollege of Biological and Food Engineering, Hubei Minzu University, 44500, Enshi, China.
Li DingCollege of Biological and Food Engineering, Hubei Minzu University, 44500, Enshi, China.
Kai LuoCollege of Biological and Food Engineering, Hubei Minzu University, 44500, Enshi, China.
Qiaoyu TangHubei Key Laboratory of Biological Resources Protection and Utilization, Hubei Minzu University, 44500, Enshi, China. 1378060165@qq.com.
Yifeng ZhouCollege of Biological and Food Engineering, Hubei Minzu University, 44500, Enshi, China. 2963754916@qq.com.
Minzu University of China · CNThe Central Hospital of Enshi Tujia and Miao Autonomous Prefecture · CN

Funding

the Enshi Autonomous Prefecture Science and Technology Program D2018009the Excellent Young and Middle-aged Scientific and Technological Innovation Team Projects of Colleges and Universities in Hubei Province T2020020the National Natural Science Foundation of China 32260070the Open Foundation of Hubei Key Laboratory of Biological Resources Protection and Utilization PT012102
6 · The paper itself

Abstract

backgroundATP sulfurylase (ATPS) is a crucial enzyme for the selenate assimilation pathway in plants.

resultsIn this study, genome-wide and comparative analyses of ATPS in Cardamine hupingshanensis, including sequence and structural analyses, were performed. The expression of ChATPS gene family members in C. hupingshanensis under selenium (Se) stress was also investigated, and our results suggest that ChATPS1-2 play key roles in the response to Se stress. Nine ATPS genes were found from C. hupingshanensis, which share highly conserved sequences with ATPS from Arabidopsis thaliana. In addition, we performed molecular docking of ATP sulfurylase in complex with compounds ATP, selenate, selenite, sulfate, and sulfite. ChAPS3-1 was found to have stronger binding energies with all compounds tested. Among these complexes, amino acid residues Arg, Gly, Ser, Glu, and Asn were commonly present.

conclusionOur study reveals the molecular mechanism of C. hupingshanensis ATP sulfurylase interacting with selenate, which is essential for understanding selenium assimilation. This information will guide further studies on the function of the ChATPS gene family in the selenium stress response and lay the foundation for the selenium metabolic pathway in higher plants.

Indexed as

ArabidopsisCardamineSeleniumAdenosine TriphosphateAmino AcidsMolecular Docking SimulationSelenic AcidSelenious AcidSulfate AdenylyltransferaseSulfatesSulfitesAdenosine TriphosphateAmino AcidsSelenic AcidSelenious AcidSeleniumSulfate AdenylyltransferaseSulfatesSulfitesATP sulfurylaseGene expressionMolecular dockingSe hyperaccumulatorsSelenium metabolism

Identifiers

PMID36253724
PMCPMC9578213
OpenAlexW4306658334

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.