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The Overexpression of Peanut (Arachis hypogaea L.) AhALDH2B6 in Soybean Enhances Cold Resistance

文献类型: 外文期刊

作者: Yang, Mingyu 1 ; Teng, Yuhan 1 ; Yue, Tong 1 ; Wang, Ziye 1 ; Feng, Guanghui 1 ; Ruan, Jingwen 1 ; Yan, Shi 1 ; Zheng, Yuhong 3 ; Zhang, Ling 3 ; Chen, Qingshan 1 ; Meng, Fanli 1 ;

作者机构: 1.Northeast Agr Univ, Coll Agr, Harbin 150030, Peoples R China

2.Agroecol Chinese Acad Sci, Northeast Inst Geog, Harbin 150081, Peoples R China

3.Jilin Acad Agr Sci, Changchun 130033, Peoples R China

关键词: soybean; transgenic breeding; ALDH; cold stress; RNA-seq

期刊名称:PLANTS-BASEL ( 影响因子:4.5; 五年影响因子:4.8 )

ISSN:

年卷期: 2023 年 12 卷 16 期

页码:

收录情况: SCI

摘要: Soybeans are the main source of oils and protein for humans and animals; however, cold stress jeopardizes their growth and limits the soybean planting area. Aldehyde dehydrogenases (ALDH) are conserved enzymes that catalyze aldehyde oxidation for detoxification in response to stress. Additionally, transgenic breeding is an efficient method for producing stress-resistant germplasms. In this study, the peanut ALDH gene AhALDH2B6 was heterologously expressed in soybean, and its function was tested. We performed RNA-seq using transgenic and wild-type soybeans with and without cold treatment to investigate the potential mechanism. Transgenic soybeans developed stronger cold tolerance, with longer roots and taller stems than P3 soybeans. Biochemically, the transgenic soybeans exhibited a decrease in malondialdehyde activity and an increase in peroxidase and catalase content, both of which are indicative of stress alleviation. They also possessed higher levels of ALDH enzyme activity. Two phenylpropanoid-related pathways were specifically enriched in up-regulated differentially expressed genes (DEGs), including the phenylpropanoid metabolic process and phenylpropanoid biosynthetic process. Our findings suggest that AhALDH2B6 specifically up-regulates genes involved in oxidoreductase-related functions such as peroxidase, oxidoreductase, monooxygenase, and antioxidant activity, which is partially consistent with our biochemical data. These findings established the function of AhALDH2B6, especially its role in cold stress processes, and provided a foundation for molecular plant breeding, especially plant-stress-resistance breeding.

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