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Elucidating the mechanism of MaGWD1-mediated starch degradation cooperatively regulated by MaMADS36 and MaMADS55 in banana

文献类型： 外文期刊

作者： Liu, Juhua 1 ; Liu, Mengting 2 ; Jia, Caihong 1 ; Zhang, Jing 1 ; Miao, Hongxia 1 ; Wang, Jingyi 1 ; Zhang, Jianbin 1 ; W 1 ;

作者机构： 1.Chinese Acad Trop Agr Sci, Inst Trop Biosci & Biotechnol, Key Lab Trop Crop Biotechnol, Minist Agr, 4 Xueyuan Rd, Haikou 571101, Hainan, Peoples R China

2.Hainan Univ, Coll Hort, Haikou 571100, Hainan, Peoples R China

3.Chinese Acad Trop Agr Sci, Hainan Acad Trop Agr Resource, 4 Xueyuan Rd, Haikou 571101, Hainan, Peoples R China

关键词： MADS-box; MaGWD1; Starch degradation; Transcriptional regulation; Banana (Musa acuminata)

期刊名称：POSTHARVEST BIOLOGY AND TECHNOLOGY （ 影响因子：5.537； 五年影响因子：5.821 ）

ISSN： 0925-5214

年卷期： 2021 年 179 卷

页码：

收录情况： SCI

摘要： Banana (Musa acuminata) is a common starch-conversion fruit. Starch is rapidly degraded and converted to soluble sugars during postharvest banana fruit ripening. The conversion efficiency directly influences fruit firmness, sweetness, and shelf life. Glucan, water dikinase (GWD) is the first rate-limiting enzyme of starch metabolism. Musa acuminata glucan water dikinase 1 (MaGWD1) plays an important role in banana starch metabolism and its expression is regulated by transcription factors (TFs). However, the regulation of MaGWD1 by MADS-box TFs remains unclear. In this study, the molecular mechanism underlying the cooperative regulation of MaGWD1-mediated starch degradation by MaMADS36 and MaMADS55 was investigated. The results indicated that MaMADS36 interacts with MaMADS55. Both MaMADS36 and MaMADS55 could directly bind to the same position on the CA/T(r)G box within the MaGWD1 promoter. MaMADS36 and MaMADS55 cooperatively regulate banana fruit starch degradation via transcriptional control of MaGWD1.These findings improve our understanding of how TFs regulate starch degradation; this information may be used for banana fruit quality improvement and to support the development of the banana industry.

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