{"title":"Bioinformatics, expression analysis, and functional verification of allene oxide synthase gene HvnAOS1 and HvnAOS2 in qingke","authors":"Likun An, Ziao Wang, Yongmei Cui, Youhua Yao, Yixiong Bai, Yuehai Liu, Xin Li, Xiaohua Yao, Kunlun Wu","doi":"10.1515/biol-2022-0855","DOIUrl":null,"url":null,"abstract":"Allene oxide synthase (AOS) is a key enzyme involved in the jasmonic acid (JA) synthesis pathway in plants. To explore its function on the regulatory mechanism of JA synthesis, we screened and identified two <jats:italic>AOS</jats:italic> genes <jats:italic>HvnAOS1</jats:italic> and <jats:italic>HvnAOS2</jats:italic> in qingke. Both HvnAOS1 and HvnAOS2 contained conserved heme-binding motif, which is most closely related to AtsAOS2, indicating controlled dehydration of fatty acid hydroperoxides to allene oxides. Molecular docking simulations identified the key amino acid sites that were important for heme binding and interaction with 13(<jats:italic>S</jats:italic>)-HPOT, respectively. The expression pattern also indicated that <jats:italic>HvnAOS1</jats:italic> and <jats:italic>HvnAOS2</jats:italic> were highly induced by JA, abscisic acid, and salicylic acid. Subcellular localization of <jats:italic>HvnAOS1</jats:italic> and <jats:italic>HvnAOS2</jats:italic> using transient expression of <jats:italic>Agrobacterium tumefaciens</jats:italic> showed the green fluorescent protein signal in the cell cytoplasm of the <jats:italic>N</jats:italic>. <jats:italic>benthamiana</jats:italic> leaves. Overexpression of <jats:italic>HvnAOS1</jats:italic> and <jats:italic>HvnAOS2</jats:italic> in <jats:italic>Arabidopsis aos</jats:italic> mutant restored male fertility and plant resistance to <jats:italic>Botrytis cinerea</jats:italic>, indicating that <jats:italic>HvnAOS1</jats:italic> and <jats:italic>HvnAOS2</jats:italic> can restore the functions of <jats:italic>AOS</jats:italic> in <jats:italic>Arabidopsis aos</jats:italic> mutant.","PeriodicalId":19605,"journal":{"name":"Open Life Sciences","volume":null,"pages":null},"PeriodicalIF":1.7000,"publicationDate":"2024-04-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Open Life Sciences","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1515/biol-2022-0855","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Allene oxide synthase (AOS) is a key enzyme involved in the jasmonic acid (JA) synthesis pathway in plants. To explore its function on the regulatory mechanism of JA synthesis, we screened and identified two AOS genes HvnAOS1 and HvnAOS2 in qingke. Both HvnAOS1 and HvnAOS2 contained conserved heme-binding motif, which is most closely related to AtsAOS2, indicating controlled dehydration of fatty acid hydroperoxides to allene oxides. Molecular docking simulations identified the key amino acid sites that were important for heme binding and interaction with 13(S)-HPOT, respectively. The expression pattern also indicated that HvnAOS1 and HvnAOS2 were highly induced by JA, abscisic acid, and salicylic acid. Subcellular localization of HvnAOS1 and HvnAOS2 using transient expression of Agrobacterium tumefaciens showed the green fluorescent protein signal in the cell cytoplasm of the N. benthamiana leaves. Overexpression of HvnAOS1 and HvnAOS2 in Arabidopsis aos mutant restored male fertility and plant resistance to Botrytis cinerea, indicating that HvnAOS1 and HvnAOS2 can restore the functions of AOS in Arabidopsis aos mutant.
期刊介绍:
Open Life Sciences (previously Central European Journal of Biology) is a fast growing peer-reviewed journal, devoted to scholarly research in all areas of life sciences, such as molecular biology, plant science, biotechnology, cell biology, biochemistry, biophysics, microbiology and virology, ecology, differentiation and development, genetics and many others. Open Life Sciences assures top quality of published data through critical peer review and editorial involvement throughout the whole publication process. Thanks to the Open Access model of publishing, it also offers unrestricted access to published articles for all users.