Two amino acid changes in the R3 repeat cause functional divergence of two clustered MYB10 genes in peach
文献类型： 外文期刊
作者： Zhou, Hui 1 ; Liao, Liao 1 ; Xu, Shengli 1 ; Ren, Fei 3 ; Zhao, Jianbo 3 ; Ogutu, Collins 1 ; Wang, Lu 1 ; Jiang, Quan 3 ; H 1 ;
作者机构： 1.Chinese Acad Sci, Key Lab Plant Germplasm Enhancement & Specialty A, Wuhan Bot Garden, Wuhan 430074, Hubei, Peoples R China
2.Univ Chinese Acad Sci, 19A Yuquanlu, Beijing 100049, Peoples R China
3.Beijing Acad Agr & Forestry Sci, Inst Forestry & Pomol, Beijing 100097, Peoples R China
4.Anhui Acad Agr Sci, Hort Inst, Key Lab Genet Improvement & Ecophysiol Hort Crops, Hefei 230031, Anhui, Peoples R China
5.Chinese Acad Sci, Sinoafrican Joint Res Ctr, Wuhan 430074, Hubei, Peoples R China
关键词： Prunus; Anthocyanin coloration; R2R3-MYB TF; bHLH gene; DNA-binding affinity; Site-directed mutation
期刊名称：PLANT MOLECULAR BIOLOGY （ 影响因子：4.076； 五年影响因子：4.89 ）
ISSN： 0167-4412
年卷期： 2018 年 98 卷 1-2 期
页码：
收录情况： SCI
摘要： R2R3-MYB genes play a pivotal role in regulating anthocyanin accumulation. Here, we report two tandemly duplicated R2R3-MYB genes in peach, PpMYB10.1 and PpMYB10.2, with the latter showing lower ability to induce anthocyanin accumulation than the former. Site-directed mutation assay revealed two amino acid changes in the R3 repeat, Arg/Lys(66) and Gly/Arg(93), responsible for functional divergence between these two PpMYB10 genes. Anthocyanin-promoting activity of PpMYB10.2 was significantly increased by a single amino acid replacement of Arg(93) with Gly(93). However, either the Gly(93) Arg(93) or Arg(66) Lys(66) substitutions alone showed little impact on anthocyanin-promoting activity of PpMYB10.1, but simultaneous substitutions caused a significant decrease. Reciprocal substitution of Arg/Gly(93) could significantly alter binding affinity to PpbHLH3, while the Arg(66) Lys(66) substitution is predicted to affect the folding of the MYB DNA-binding domain, instead of PpbHLH3-binding affinity. Overall, the change of anthocyanin-promoting activity was accompanied with that of bHLH-binding affinity, suggesting that DNA-binding affinity of R2R3-MYBs depends on their bHLH partners. Our study is helpful for understanding of functional evolution of R2R3-MYBs and their interaction with DNA targets.
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