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Effects of conserved Arg20, Glu74 and Asp77 on the structure and function of a tau class glutathione S-transferase in rice
Yang, Xue1; Wu, Zhihai; Gao, Jie2,3
2021
发表期刊PLANT MOLECULAR BIOLOGY
ISSN0167-4412
卷号105期号:4-5页码:451-462
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.
关键词Glutathione S-transferases Domain interaction Linker region Site-directed mutagenesis Structural changes Activity changes
学科领域Biochemistry & Molecular Biology ; Plant Sciences
DOI10.1007/s11103-020-01099-4
收录类别SCI
语种英语
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)
WOS记录号WOS:000604193300001
出版者SPRINGER
文献子类Article
出版地DORDRECHT
EISSN1573-5028
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]
作者邮箱wuzhihai1116@163.com ; gaojie@xtbg.org.cn
引用统计
被引频次:4[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符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
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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.
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