Plant Physiology
Abstract
Disulfide bonds are essential for thefoldingof the eukaryotic secretory and membrane proteins in theendoplasmic reticulum(ER), and ER oxidoreductin-1 (Ero1) and its homologs are the major disulfide donors that supply oxidizing equivalents in the ER. Although Ero1 homologs in yeast (Saccharomyces cerevisiae) and mammals have been extensively studied, the mechanisms of plant Ero1 functions are far less understood. Here, we found that both Arabidopsis (Arabidopsis thaliana) ERO1 and its homologAtERO2are required foroxidativeprotein foldingin the ER. The outer active site, the inner active site and a long-range non-catalytic disulfide bond are required forAtERO1's function. Interestingly,AtERO1andAtERO2alsoexhibitsignificantdifferences. The ero1 plants are more sensitive to reductive stress than the ero2 plants. In vivo, bothAtERO1andAtERO2have two distinct oxidized isoforms (Ox1 and Ox2), which are determined by the formation or breakage of the putative regulatory disulfide.AtERO1is mainly present in the Ox1 redox state, while moreAtERO2exists in the Ox2 state. Furthermore,AtERO1showed much strongeroxidativeprotein foldingactivity thanAtERO2in vitro. Taken together, bothAtERO1andAtERO2are required to regulate efficient and faithfuloxidativeprotein foldingin the ER, butAtERO1may serves as the primary sulfhydryl oxidase relative toAtERO2.
| 论文编号: | DOI:10.1104/pp.19.00020 |
| 论文题目: | AtERO1 and AtERO2 Exhibit Differences in Catalyzing Oxidative Protein Folding in the Endoplasmic Reticulum |
| 英文论文题目: | AtERO1 and AtERO2 Exhibit Differences in Catalyzing Oxidative Protein Folding in the Endoplasmic Reticulum |
| 第一作者: | Fenggui Fan, Yini Zhang. Guozhong Huang, Qiao Zhang, Chih-chen Wang, Lei Wang, Dongping Lu. |
| 英文第一作者: | Fenggui Fan, Yini Zhang. Guozhong Huang, Qiao Zhang, Chih-chen Wang, Lei Wang, Dongping Lu. |
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| 发表年度: | 2019-06-04 |
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| 摘要: | Disulfide bonds are essential for thefoldingof the eukaryotic secretory and membrane proteins in theendoplasmic reticulum(ER), and ER oxidoreductin-1 (Ero1) and its homologs are the major disulfide donors that supply oxidizing equivalents in the ER. Although Ero1 homologs in yeast (Saccharomyces cerevisiae) and mammals have been extensively studied, the mechanisms of plant Ero1 functions are far less understood. Here, we found that both Arabidopsis (Arabidopsis thaliana) ERO1 and its homologAtERO2are required foroxidativeprotein foldingin the ER. The outer active site, the inner active site and a long-range non-catalytic disulfide bond are required forAtERO1's function. Interestingly,AtERO1andAtERO2alsoexhibitsignificantdifferences. The ero1 plants are more sensitive to reductive stress than the ero2 plants. In vivo, bothAtERO1andAtERO2have two distinct oxidized isoforms (Ox1 and Ox2), which are determined by the formation or breakage of the putative regulatory disulfide.AtERO1is mainly present in the Ox1 redox state, while moreAtERO2exists in the Ox2 state. Furthermore,AtERO1showed much strongeroxidativeprotein foldingactivity thanAtERO2in vitro. Taken together, bothAtERO1andAtERO2are required to regulate efficient and faithfuloxidativeprotein foldingin the ER, butAtERO1may serves as the primary sulfhydryl oxidase relative toAtERO2. |
| 英文摘要: | Disulfide bonds are essential for thefoldingof the eukaryotic secretory and membrane proteins in theendoplasmic reticulum(ER), and ER oxidoreductin-1 (Ero1) and its homologs are the major disulfide donors that supply oxidizing equivalents in the ER. Although Ero1 homologs in yeast (Saccharomyces cerevisiae) and mammals have been extensively studied, the mechanisms of plant Ero1 functions are far less understood. Here, we found that both Arabidopsis (Arabidopsis thaliana) ERO1 and its homologAtERO2are required foroxidativeprotein foldingin the ER. The outer active site, the inner active site and a long-range non-catalytic disulfide bond are required forAtERO1's function. Interestingly,AtERO1andAtERO2alsoexhibitsignificantdifferences. The ero1 plants are more sensitive to reductive stress than the ero2 plants. In vivo, bothAtERO1andAtERO2have two distinct oxidized isoforms (Ox1 and Ox2), which are determined by the formation or breakage of the putative regulatory disulfide.AtERO1is mainly present in the Ox1 redox state, while moreAtERO2exists in the Ox2 state. Furthermore,AtERO1showed much strongeroxidativeprotein foldingactivity thanAtERO2in vitro. Taken together, bothAtERO1andAtERO2are required to regulate efficient and faithfuloxidativeprotein foldingin the ER, butAtERO1may serves as the primary sulfhydryl oxidase relative toAtERO2. |
| 刊物名称: | Plant Physiology |
| 英文刊物名称: | Plant Physiology |
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| 其它备注: | Fenggui Fan, Yini Zhang. Guozhong Huang, Qiao Zhang, Chih-chen Wang, Lei Wang, Dongping Lu. AtERO1 and AtERO2 Exhibit Differences in Catalyzing Oxidative Protein Folding in the Endoplasmic Reticulum. Plant Physiology. DOI:10.1104/pp.19.00020 |
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