文献类型： 外文期刊
作者： Huang, Ting 1 ; Zheng, Ting 2 ; Hong, Pingjing 5 ; He, Jianjun 4 ; Cheng, Yuanxin 1 ; Yang, Jungui 1 ; Zhou, Yunzhi 1 ; Wang, Bo 1 ; Zhou, Sihong 1 ; Cheng, Guo 3 ; Jia, Haifeng 1 ;
作者机构： 1.Guangxi Univ, Coll Agr, 100 Daxue Rd, Nanning 530004, Guangxi, Peoples R China
2.Zhejiang Acad Agr Sci, Inst Hort, Hangzhou 310021, Peoples R China
3.Guangxi Acad Agr Sci, Grape & Wine Res Inst, Nanning, Peoples R China
4.Guangxi Acad Special Crops, Lab Germplasm Innovat & Utilizat Specialized Econ, Guilin 541004, Guangxi, Peoples R China
5.Nanjing Agr Univ, Coll Hort, Key Lab Genet & Fruit Dev, 1st Weigang Rd, Nanjing 210095, Peoples R China
关键词： Grapes; VvSS3; ABA; VvSnRK1 beta; Transgene
期刊名称：PLANT PHYSIOLOGY AND BIOCHEMISTRY （ 影响因子：5.7； 五年影响因子：6.4 ）
ISSN： 0981-9428
年卷期： 2025 年 221 卷
页码：
收录情况： SCI
摘要： Sucrose synthase (SS) is one of the key functional enzymes involved in sugar metabolism in plants, and its activity can directly affect sugar accumulation, thereby influencing fruit quality. Our previous research found an interaction between VvSS3 and VvSnRK1 beta. In this study, we discovered that SS enzyme activity was mainly oriented towards decomposition, with the highest activity occurring before the veraison stage, and the overall trend of SS enzyme activity changes was positively correlated with exogenous ABA concentration. Site-directed mutagenesis revealed that VvSS3S176 and VvSS3S381 were crucial sites for the interaction between VvSS3 and VvSnRK1 beta. Subcellular localization results showed that VvSS3S176 and VvSS3S381, as well as VvSS3, were located on the cell membrane. VvSS3 was sensitive to ABA, promoting the accumulation of soluble sugars and anthocyanins in transgenic callus, increasing endogenous ABA content, and reducing organic acid components. VvSS3S176 and VvSS3S381 only altered the activity of SS in the synthesis direction, while the transcription level of VvSnRK1 beta in transgenic callus significantly decreased. After exogenous ABA treatment, Ser176 and Ser381 reduced the inhibition of VvSS3 on VvSnRK1 beta expression. Mutation of the binding sites of VvSS3 prevented the formation of complexes VvSnRK1 beta-VvSS3, thus interfering with downstream metabolism. This suggests that VvSnRK1 beta may form a protein complex by interacting with VvSS3, participating in the accumulation of soluble sugars in grape fruits mediated by ABA response.
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