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Demyristoylation of the Cytoplasmic Redox Protein Trx-h2 Is Critical for Inducing a Rapid Cold Stress Response in Plants

by Phan, Kieu Anh Thi , Bae, Su Bin , Wi, Seong Dong , Kim, Min Gab , Yun, Dae-Jin , Chae, Ho Byoung , Park, Joung Hun , Kim, Woe-Yeon , Kwak, Sang-Soo , Lee, Eun Seon , Lee, Sang Yeol , Paeng, Seol Ki

in Alanine / Antibodies / Antioxidants / Arabidopsis / C-repeat binding factors (CBFs) / Cell division / Cloning / Cold / cold shock response / cold stress / Cold tolerance / cold/freezing stress / fatty acids / Genes / Homeostasis / Localization / mutants / Myristoylation / myristoylation/demyristoylation / Nitrogen / nuclear translocation / Nuclear transport / Plasmids / Point mutation / Proteins / temperature / Thioredoxin / thioredoxin h2 / thioredoxins / Trx-h2(G/A) point mutation variant

2021

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Demyristoylation of the Cytoplasmic Redox Protein Trx-h2 Is Critical for Inducing a Rapid Cold Stress Response in Plants

2021

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Demyristoylation of the Cytoplasmic Redox Protein Trx-h2 Is Critical for Inducing a Rapid Cold Stress Response in Plants

2021

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Journal Article

Demyristoylation of the Cytoplasmic Redox Protein Trx-h2 Is Critical for Inducing a Rapid Cold Stress Response in Plants

Phan, Kieu Anh Thi,

Bae, Su Bin,

Wi, Seong Dong,

Kim, Min Gab,

Yun, Dae-Jin,

Chae, Ho Byoung,

Park, Joung Hun,

Kim, Woe-Yeon,

Kwak, Sang-Soo,

Lee, Eun Seon,

Lee, Sang Yeol,

Paeng, Seol Ki

2021

Overview

In Arabidopsis, the cytosolic redox protein thioredoxin h2 (Trx-h2) is anchored to the cytoplasmic endomembrane through the myristoylated second glycine residue (Gly2). 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 cold-responsive (COR) 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 trx-h2 mutant background, overexpressing Trx-h2 (Trx-h2OE/trx-h2) and its point mutation variant Trx-h2(G/A) [Trx-h2(G/A)OE/trx-h2], in which the Gly2 was replaced by alanine (Ala). Due to the lack of Gly2, 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, COR genes were up-regulated earlier in Trx-h2(G/A)2OE/trx-h2 plants than in Trx-h2OE/trx-h2 plants under cold stress. Consequently, Trx-h2(G/A)2OE/trx-h2 plants showed greater cold tolerance than Col-0 (wild type) and Trx-h2OE/trx-h2 plants. Overall, our results clearly demonstrate the significance of the demyristoylation of Trx-h2 in enhancing plant cold/freezing tolerance.

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Publisher

MDPI AG,MDPI

Subject

/ C-repeat binding factors (CBFs)

/ Cell division

/ Cloning