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Mol. Cells 2009; 28(4): 383-388

Published online October 31, 2009

https://doi.org/10.1007/s10059-009-0154-4

© The Korean Society for Molecular and Cellular Biology

Identification of Potential DREB2C Targets in Arabidopsis thaliana Plants Overexpressing DREB2C Using Proteomic Analysis

Kyunghee Lee, Ki Soo Han, Young Sang Kwon, Jung Han Lee, Sun Ho Kim, Woo Sik Chung,
Yujung Kim, Sung-Sik Chun, Hee Kyu Kim, and Dong-Won Bae

Received: July 13, 2009; Revised: September 15, 2009; Accepted: September 21, 2009

Abstract

The dehydration responsive element binding protein 2C (DREB2C) is a dehydration responsive element/C-repeat (DRE/CRT)-motif binding transcription factor that induced by mild heat stress. Previous experiments established that overexpression of DREB2C cDNA driven by the cauliflower mosaic virus 35S promoter (35S:DREB2C) resulted in increased heat tolerance in Arabidopsis. We first analyzed the proteomic profiles in wild-type and 35S:DREB2C plants at a normal temperature (22°C), but could not detect any differences between the proteomes of wild-type and 35S: DREB2C plants. The transcript level of DREB2C in 35S: DREB2C plants after treatment with mild heat stress was increased more than two times compared with expres-sion in 35S:DREB2C plants under unstressed condition. A proteomic approach was used to decipher the molecular mechanisms underlying thermotolerance in 35S:DREB2C Arabidopsis plants. Eleven protein spots were identified as being differentially regulated in 35S:DREB2C plants. Moreover, in silico motif analysis showed that peptidyl-prolyl isomerase ROC4, glutathione transferase 8, pyridoxal biosynthesis protein PDX1, and elongation factor Tu contained one or more DRE/CRT motifs. To our knowledge, this study is the first to identify possible targets of DREB2C transcription factors at the protein level. The proteomic results were in agreement with transcriptional data.

Keywords , dehydration responsive element, DREB2C, proteomic analysis, thermotolerance

Article

Research Article

Mol. Cells 2009; 28(4): 383-388

Published online October 31, 2009 https://doi.org/10.1007/s10059-009-0154-4

Copyright © The Korean Society for Molecular and Cellular Biology.

Identification of Potential DREB2C Targets in Arabidopsis thaliana Plants Overexpressing DREB2C Using Proteomic Analysis

Kyunghee Lee, Ki Soo Han, Young Sang Kwon, Jung Han Lee, Sun Ho Kim, Woo Sik Chung,
Yujung Kim, Sung-Sik Chun, Hee Kyu Kim, and Dong-Won Bae

Received: July 13, 2009; Revised: September 15, 2009; Accepted: September 21, 2009

Abstract

The dehydration responsive element binding protein 2C (DREB2C) is a dehydration responsive element/C-repeat (DRE/CRT)-motif binding transcription factor that induced by mild heat stress. Previous experiments established that overexpression of DREB2C cDNA driven by the cauliflower mosaic virus 35S promoter (35S:DREB2C) resulted in increased heat tolerance in Arabidopsis. We first analyzed the proteomic profiles in wild-type and 35S:DREB2C plants at a normal temperature (22°C), but could not detect any differences between the proteomes of wild-type and 35S: DREB2C plants. The transcript level of DREB2C in 35S: DREB2C plants after treatment with mild heat stress was increased more than two times compared with expres-sion in 35S:DREB2C plants under unstressed condition. A proteomic approach was used to decipher the molecular mechanisms underlying thermotolerance in 35S:DREB2C Arabidopsis plants. Eleven protein spots were identified as being differentially regulated in 35S:DREB2C plants. Moreover, in silico motif analysis showed that peptidyl-prolyl isomerase ROC4, glutathione transferase 8, pyridoxal biosynthesis protein PDX1, and elongation factor Tu contained one or more DRE/CRT motifs. To our knowledge, this study is the first to identify possible targets of DREB2C transcription factors at the protein level. The proteomic results were in agreement with transcriptional data.

Keywords: , dehydration responsive element, DREB2C, proteomic analysis, thermotolerance

Mol. Cells
Aug 31, 2022 Vol.45 No.8, pp. 513~602
COVER PICTURE
Cryo-EM structure of human porphyrin transporter ABCB6 (main figure) shows that binding of hemin (inset, magenta) in concert with two glutathione molecules (cyan) primes ABCB6 for high ATP turnover (Kim et al., pp. 575-587).

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