Effects of conserved Arg20, Glu74 and Asp77 on the structure and function of a tau class glutathione S-transferase in rice
文献类型：期刊论文
| 作者 | Yang, Xue1; Wu, Zhihai; Gao, Jie2,3 |
| 刊名 | PLANT MOLECULAR BIOLOGY
 |
| 出版日期 | 2021 |
| 卷号 | 105期号:4-5页码:451-462 |
| ISSN号 | 0167-4412 |
| 关键词 | Glutathione S-transferases Domain interaction Linker region Site-directed mutagenesis Structural changes Activity changes |
| DOI | 10.1007/s11103-020-01099-4 |
| 文献子类 | Article |
| 英文摘要 | Key message The relative position of domains is critical for enzymatic properties of tau class glutathione S-transferases, and altering the position of linker far away from the active center affects catalytic property. Glutathione S-transferases (GSTs) are a family of phase II detoxification enzymes whose main function is to improve plant resistance to stresses. To understand the structural effects of tau class GSTs on their function, using OsGSTU17 as an example, we predicted the residues involved in the interactions between its domains and linker region. We further detected the structural changes in mutants and the corresponding changes in terms of substrate activity and kinetic parameters. Four pairs of residues, including Ala14 and Trp165, Arg20 and Tyr154, Glu74 and Arg98, Asp77 and Met87, forming hydrogen bonds and salt bridges were found to play important roles in maintaining the relative position between the domains and linker region inside the protein. The hydrogen bond between Trp165 and Ala14 affected the structural stability has been demonstrated in our previous study. The mutant R20A lost almost all catalytic activity. Interestingly, the mutant E74A exhibited a significant decrease in activity towards 7-chloro-4-nitrobenzo-2-oxa-1, 3-diazole, 1-chloro-2, 4-dinitrobenzene and 4-nitrobenzyl chloride, while its activity towards substrate cumene hydroperoxide remained unchanged. Compared with other mutants, the mutant D77A exhibited decreased affinity to its substrates and increased activity towards 1-chloro-2, 4-dinitrobenzene and cumene hydroperoxide, but its thermodynamic stability did not change significantly. The relative position of individual domain was critical for enzymatic properties, and the linker which is far away from the active site could change the enzymatic properties of GSTs via altering the relative position of the individual domain. Our results provide insights into the relationship between structure and function of tau class GSTs. |
| 学科主题 | Biochemistry & Molecular Biology ; Plant Sciences |
| 电子版国际标准刊号 | 1573-5028 |
| 出版地 | DORDRECHT |
| WOS关键词 | TRANSGENIC TOBACCO SEEDLINGS ; SUBUNIT INTERFACE RESIDUES ; CIRCULAR-DICHROISM SPECTRA ; CATALYTIC MECHANISM ; ROLES ; SITE ; CONFORMATION ; EVOLUTION ; SULFONATE ; GROWTH |
| WOS研究方向 | Science Citation Index Expanded (SCI-EXPANDED) |
| 语种 | 英语 |
| 出版者 | SPRINGER |
| WOS记录号 | WOS:000604193300001 |
| 资助机构 | National Key R&D Program of Ministry of Agriculture and Rural Affairs of the People's Republic of China [2018YFD0300207-2] ; Department of Science and Technology of Jilin Province [20190301061NY] |
| 源URL | [http://ir.ibcas.ac.cn/handle/2S10CLM1/26453]  |
| 专题 | 系统与进化植物学国家重点实验室 |
| 作者单位 | 1.Jilin Agr Univ, Coll Life Sci, Changchun 130118, Peoples R China 2.Chinese Acad Sci, Inst Bot, State Key Lab Systemat & Evolutionary Bot, Beijing 100093, Peoples R China 3.Chinese Acad Sci, Xishuangbanna Trop Bot Garden, CAS Key Lab Trop Forest Ecol, Menglun 666303, Yunnan, Peoples R China 4.Chinese Acad Sci, Core Bot Gardens, Ctr Conservat Biol, Mengla 666303, Peoples R China |
| 推荐引用方式 GB/T 7714 | Yang, Xue,Wu, Zhihai,Gao, Jie. Effects of conserved Arg20, Glu74 and Asp77 on the structure and function of a tau class glutathione S-transferase in rice[J]. PLANT MOLECULAR BIOLOGY,2021,105(4-5):451-462. |
| APA | Yang, Xue,Wu, Zhihai,&Gao, Jie.(2021).Effects of conserved Arg20, Glu74 and Asp77 on the structure and function of a tau class glutathione S-transferase in rice.PLANT MOLECULAR BIOLOGY,105(4-5),451-462. |
| MLA | Yang, Xue,et al."Effects of conserved Arg20, Glu74 and Asp77 on the structure and function of a tau class glutathione S-transferase in rice".PLANT MOLECULAR BIOLOGY 105.4-5(2021):451-462. |
入库方式： OAI收割
来源：植物研究所
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