| 茶树黄金芽CsHIPP26.1蛋白螯合离子的筛选与鉴定 |
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| 引用本文： | 刘富浩,范延艮,王域,孟凡月,张丽霞. 茶树黄金芽CsHIPP26.1蛋白螯合离子的筛选与鉴定[J]. 茶叶科学, 2022, 42(2): 179-186. DOI: 10.3969/j.issn.1000-369X.2022.02.003 |
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| 作者姓名： | 刘富浩 范延艮 王域 孟凡月 张丽霞 |
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| 作者单位： | 1.山东农业大学园艺科学与工程学院,山东 泰安 271018; 2.作物生物学国家重点实验室,山东 泰安 271018 |
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| 基金项目： | 山东省现代农业产业技术体系创新团队项目（SDAIT-19-05）； |
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| 摘 要： | 重金属相关异戊二烯化植物蛋白(HIPPs)由于其独特的重金属结合域和异戊二烯序列的结构特点,成为一类重要的金属分子伴侣.为鉴定茶树(Camellia sinensis)黄金芽CsHIPP26.1蛋白的螯合离子,将pET-32a-CsHIPP26.1重组质粒和空载体分别转入大肠杆菌BL21,在分别添加4 mol·L-1的...
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| 关 键 词： | 重金属异戊二烯植物蛋白 CsHIPP26.1 金属离子 茶树 |
| 收稿时间： | 2021-12-06 |
Screening and Identification of Chaperone CsHIPP26.1 Chelating Ions in Tea Cultivar 'Huangjinya' |
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| LIU Fuhao,FAN Yangen,WANG Yu,MENG Fanyue,ZHANG Lixia. Screening and Identification of Chaperone CsHIPP26.1 Chelating Ions in Tea Cultivar 'Huangjinya'[J]. Journal of Tea Science, 2022, 42(2): 179-186. DOI: 10.3969/j.issn.1000-369X.2022.02.003 |
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| Authors: | LIU Fuhao FAN Yangen WANG Yu MENG Fanyue ZHANG Lixia |
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| Affiliation: | 1. College of Horticulture Science and Engineering, Tai'an 271018, China; 2. State Key Laboratory of Crop Biology, Shandong Agricultural University, Tai'an 271018, China |
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| Abstract: | Heavy metal-associated isoprenylated plant proteins (HIPPs) is an important metallochaperones due to its unique heavy metal binding domains (HMA) and the structural characteristics of isoprenylation motif. In order to identify the chelating ions of CsHIPP26.1 protein in Camellia sinensis (L.) cv. ‘Huangjinya’, the pET-32a-CsHIPP26.1 recombinant plasmids and empty carriers were respectively transferred into E. coli BL21, and then were cultured in LB liquid culture medium with 4 mol·L-1 single metal ions (CuCl2, ZnCl2, MgCl2, FeCl3, CaCl2) or multiple metal ions and 1 mmol·L-1 IPTG. The growth of E. coli in different ion media was observed, meanwhile the fusion target protein was obtained by His-tag protein purification magnetic bead. The contents of metal ions in fusion protein were analyzed by atomic absorption spectrophotometer, and the number of ions chelated by the protein was calculated. The results show that CsHIPP26.1 protein was only chelated with Zn2+ and Cu2+, and the chelating ability to Zn2+ was significantly higher than Cu2+. Based on the molar ratio of its bound metal ions to the target protein, the maximum number of Zn2+, Cu2+ chelated by CsHIPP26.1 protein was 2 and 1, respectively. |
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| Keywords: | heavy metal-associated isoprenylated plant protein CsHIPP26.1 metal ions Camellia sinensis |
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