Demyristoylation of the Cytoplasmic Redox Protein Trx-h2 Is Critical for Inducing a Rapid Cold Stress Response in Plants
In Arabidopsis, the cytosolic redox protein thioredoxin h2 (Trx-h2) is anchored to the cytoplasmic endomembrane through the myristoylated second glycine residue (Gly<sup>2</sup>). However, under cold stress, the cytosolic Trx-h2 is rapidly translocated to the nucleus, where it interacts...
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| Format: | Article |
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MDPI AG
2021-08-01
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| Series: | Antioxidants |
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| Online Access: | https://www.mdpi.com/2076-3921/10/8/1287 |
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| author | Eun Seon Lee Joung Hun Park Seong Dong Wi Ho Byoung Chae Seol Ki Paeng Su Bin Bae Kieu Anh Thi Phan Min Gab Kim Sang-Soo Kwak Woe-Yeon Kim Dae-Jin Yun Sang Yeol Lee |
| author_facet | Eun Seon Lee Joung Hun Park Seong Dong Wi Ho Byoung Chae Seol Ki Paeng Su Bin Bae Kieu Anh Thi Phan Min Gab Kim Sang-Soo Kwak Woe-Yeon Kim Dae-Jin Yun Sang Yeol Lee |
| author_sort | Eun Seon Lee |
| collection | DOAJ |
| description | In Arabidopsis, the cytosolic redox protein thioredoxin h2 (Trx-h2) is anchored to the cytoplasmic endomembrane through the myristoylated second glycine residue (Gly<sup>2</sup>). However, under cold stress, the cytosolic Trx-h2 is rapidly translocated to the nucleus, where it interacts with and reduces the cold-responsive C-repeat-binding factors (CBFs), thus activating <i>cold-responsive (COR)</i> genes. In this study, we investigated the significance of fatty acid modification of Trx-h2 under cold conditions by generating transgenic Arabidopsis lines in the <i>trx-h2</i> mutant background, overexpressing <i>Trx-h2</i> (Trx-h2<sup>OE</sup>/<i>trx-h2</i>) and its point mutation variant <i>Trx-h2(G/A)</i> [Trx-h2(G/A)<sup>OE</sup>/<i>trx-h2</i>], in which the Gly<sup>2</sup> was replaced by alanine (Ala). Due to the lack of Gly<sup>2</sup>, Trx-h2(G/A) was incapable of myristoylation, and a part of Trx-h2(G/A) localized to the nucleus even under warm temperature. As no time is spent on the demyristoylation and subsequent nuclear translocation of Trx-h2(G/A) under a cold snap, the ability of Trx-h2(G/A) to protect plants from cold stress was greater than that of Trx-h2. Additionally, <i>COR</i> genes were up-regulated earlier in Trx-h2(G/A)2<sup>OE</sup>/<i>trx-h2 </i>plants than in Trx-h2<sup>OE</sup>/<i>trx-h2 </i>plants under cold stress. Consequently, Trx-h2(G/A)2<sup>OE</sup>/<i>trx-h2 </i>plants showed greater cold tolerance than Col-0 (wild type) and Trx-h2<sup>OE</sup>/<i>trx-h2 </i>plants. Overall, our results clearly demonstrate the significance of the demyristoylation of Trx-h2 in enhancing plant cold/freezing tolerance. |
| first_indexed | 2024-03-10T09:03:23Z |
| format | Article |
| id | doaj.art-7e8cc7fb5fc743dba1f3d2f155e8f441 |
| institution | Directory Open Access Journal |
| issn | 2076-3921 |
| language | English |
| last_indexed | 2024-03-10T09:03:23Z |
| publishDate | 2021-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antioxidants |
| spelling | doaj.art-7e8cc7fb5fc743dba1f3d2f155e8f4412023-11-22T06:36:56ZengMDPI AGAntioxidants2076-39212021-08-01108128710.3390/antiox10081287Demyristoylation of the Cytoplasmic Redox Protein Trx-h2 Is Critical for Inducing a Rapid Cold Stress Response in PlantsEun Seon Lee0Joung Hun Park1Seong Dong Wi2Ho Byoung Chae3Seol Ki Paeng4Su Bin Bae5Kieu Anh Thi Phan6Min Gab Kim7Sang-Soo Kwak8Woe-Yeon Kim9Dae-Jin Yun10Sang Yeol Lee11Division of Applied Life Science (BK21+) and PMBBRC, Gyeongsang National University, Jinju 52828, KoreaDivision of Applied Life Science (BK21+) and PMBBRC, Gyeongsang National University, Jinju 52828, KoreaDivision of Applied Life Science (BK21+) and PMBBRC, Gyeongsang National University, Jinju 52828, KoreaDivision of Applied Life Science (BK21+) and PMBBRC, Gyeongsang National University, Jinju 52828, KoreaDivision of Applied Life Science (BK21+) and PMBBRC, Gyeongsang National University, Jinju 52828, KoreaDivision of Applied Life Science (BK21+) and PMBBRC, Gyeongsang National University, Jinju 52828, KoreaDivision of Applied Life Science (BK21+) and PMBBRC, Gyeongsang National University, Jinju 52828, KoreaCollege of Pharmacy, Gyeongsang National University, Jinju 52828, KoreaPlant Systems Engineering Research Center, KRIBB, Daejeon 34141, KoreaDivision of Applied Life Science (BK21+) and PMBBRC, Gyeongsang National University, Jinju 52828, KoreaDepartment of Biomedical Science & Engineering, Konkuk University, Seoul 05029, KoreaDivision of Applied Life Science (BK21+) and PMBBRC, Gyeongsang National University, Jinju 52828, KoreaIn Arabidopsis, the cytosolic redox protein thioredoxin h2 (Trx-h2) is anchored to the cytoplasmic endomembrane through the myristoylated second glycine residue (Gly<sup>2</sup>). However, under cold stress, the cytosolic Trx-h2 is rapidly translocated to the nucleus, where it interacts with and reduces the cold-responsive C-repeat-binding factors (CBFs), thus activating <i>cold-responsive (COR)</i> genes. In this study, we investigated the significance of fatty acid modification of Trx-h2 under cold conditions by generating transgenic Arabidopsis lines in the <i>trx-h2</i> mutant background, overexpressing <i>Trx-h2</i> (Trx-h2<sup>OE</sup>/<i>trx-h2</i>) and its point mutation variant <i>Trx-h2(G/A)</i> [Trx-h2(G/A)<sup>OE</sup>/<i>trx-h2</i>], in which the Gly<sup>2</sup> was replaced by alanine (Ala). Due to the lack of Gly<sup>2</sup>, Trx-h2(G/A) was incapable of myristoylation, and a part of Trx-h2(G/A) localized to the nucleus even under warm temperature. As no time is spent on the demyristoylation and subsequent nuclear translocation of Trx-h2(G/A) under a cold snap, the ability of Trx-h2(G/A) to protect plants from cold stress was greater than that of Trx-h2. Additionally, <i>COR</i> genes were up-regulated earlier in Trx-h2(G/A)2<sup>OE</sup>/<i>trx-h2 </i>plants than in Trx-h2<sup>OE</sup>/<i>trx-h2 </i>plants under cold stress. Consequently, Trx-h2(G/A)2<sup>OE</sup>/<i>trx-h2 </i>plants showed greater cold tolerance than Col-0 (wild type) and Trx-h2<sup>OE</sup>/<i>trx-h2 </i>plants. Overall, our results clearly demonstrate the significance of the demyristoylation of Trx-h2 in enhancing plant cold/freezing tolerance.https://www.mdpi.com/2076-3921/10/8/1287thioredoxin h2myristoylation/demyristoylationnuclear translocationC-repeat binding factors (CBFs)cold/freezing stressTrx-h2(G/A) point mutation variant |
| spellingShingle | Eun Seon Lee Joung Hun Park Seong Dong Wi Ho Byoung Chae Seol Ki Paeng Su Bin Bae Kieu Anh Thi Phan Min Gab Kim Sang-Soo Kwak Woe-Yeon Kim Dae-Jin Yun Sang Yeol Lee Demyristoylation of the Cytoplasmic Redox Protein Trx-h2 Is Critical for Inducing a Rapid Cold Stress Response in Plants Antioxidants thioredoxin h2 myristoylation/demyristoylation nuclear translocation C-repeat binding factors (CBFs) cold/freezing stress Trx-h2(G/A) point mutation variant |
| title | Demyristoylation of the Cytoplasmic Redox Protein Trx-h2 Is Critical for Inducing a Rapid Cold Stress Response in Plants |
| title_full | Demyristoylation of the Cytoplasmic Redox Protein Trx-h2 Is Critical for Inducing a Rapid Cold Stress Response in Plants |
| title_fullStr | Demyristoylation of the Cytoplasmic Redox Protein Trx-h2 Is Critical for Inducing a Rapid Cold Stress Response in Plants |
| title_full_unstemmed | Demyristoylation of the Cytoplasmic Redox Protein Trx-h2 Is Critical for Inducing a Rapid Cold Stress Response in Plants |
| title_short | Demyristoylation of the Cytoplasmic Redox Protein Trx-h2 Is Critical for Inducing a Rapid Cold Stress Response in Plants |
| title_sort | demyristoylation of the cytoplasmic redox protein trx h2 is critical for inducing a rapid cold stress response in plants |
| topic | thioredoxin h2 myristoylation/demyristoylation nuclear translocation C-repeat binding factors (CBFs) cold/freezing stress Trx-h2(G/A) point mutation variant |
| url | https://www.mdpi.com/2076-3921/10/8/1287 |
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