OsCBE1, a Substrate Receptor of Cullin4-Based E3 Ubiquitin Ligase, Functions as a Regulator of Abiotic Stress Response and Productivity in Rice
Ubiquitination is an important environmental stress response, and E3 ubiquitin ligases play a major role in the process. T-DNA insertion mutants of rice, <i>Oscbe1-1</i>, and <i>Oscbe1-2,</i> were identified through the screening of cold stress tolerance at seedling stage. &l...
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doaj-80e22a1fbad24567b296fbb5b60066d62021-03-03T00:00:50ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-03-01222487248710.3390/ijms22052487OsCBE1, a Substrate Receptor of Cullin4-Based E3 Ubiquitin Ligase, Functions as a Regulator of Abiotic Stress Response and Productivity in RiceJuyoung Choi0Wonkyung Lee1Gynheung An2Seong-Ryong Kim3Department of Life Science, Sogang University, Seoul 04107, KoreaDepartment of Life Science, Sogang University, Seoul 04107, KoreaDepartment of Plant Molecular Systems Biotechnology, Kyung Hee University, Yongin 17104, KoreaDepartment of Life Science, Sogang University, Seoul 04107, KoreaUbiquitination is an important environmental stress response, and E3 ubiquitin ligases play a major role in the process. T-DNA insertion mutants of rice, <i>Oscbe1-1</i>, and <i>Oscbe1-2,</i> were identified through the screening of cold stress tolerance at seedling stage. <i>O</i>s<i>cbe1</i> mutants showed a significantly higher cold stress tolerance in the fresh weight, chlorophyll content, and photosynthetic efficiency than wild type. Molecular prediction showed that <i>OsCBE1</i> (<i>Oryza sativa</i> Cullin4-Based E3 ubiquitin ligase1) encoded a novel substrate receptor of Cullin4-based E3 ubiquitin ligase complex (C4E3). Whereas <i>Oscbe1</i> mutants had fewer panicles and grains than wild type in the paddy field, the overexpression lines of <i>OsCBE1</i> had more panicles and grains, suggesting that <i>OsCBE1</i> is involved in the regulation of both abiotic stress response and development. <i>Oscbe1</i> mutants also showed ABA hypersensitivity during seed germination, suggesting <i>OsCBE1</i> function for the stress response via ABA signaling. In silico analysis of OsCBE1 activity predicted a CCCH-type transcription factor, OsC3H32, as a putative substrate. Co-IP (Co-immunoprecipitation) study showed that OsCBE1 interacts with OsDDB1, an expected binding component of OsCBE1 and OsC3H32. Additionally, expression of <i>OsOLE16, OsOLE18</i>, and <i>OsBURP5</i> were negatively related with expression of <i>OsCBE1</i>. These results suggest that <i>OsCBE1</i> functions as a regulator of the abiotic stress response via CCCH as a member of the C4E3.https://www.mdpi.com/1422-0067/22/5/2487abiotic stresscullin4crop productivityE3 ubiquitin ligaserice |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Juyoung Choi Wonkyung Lee Gynheung An Seong-Ryong Kim |
spellingShingle |
Juyoung Choi Wonkyung Lee Gynheung An Seong-Ryong Kim OsCBE1, a Substrate Receptor of Cullin4-Based E3 Ubiquitin Ligase, Functions as a Regulator of Abiotic Stress Response and Productivity in Rice International Journal of Molecular Sciences abiotic stress cullin4 crop productivity E3 ubiquitin ligase rice |
author_facet |
Juyoung Choi Wonkyung Lee Gynheung An Seong-Ryong Kim |
author_sort |
Juyoung Choi |
title |
OsCBE1, a Substrate Receptor of Cullin4-Based E3 Ubiquitin Ligase, Functions as a Regulator of Abiotic Stress Response and Productivity in Rice |
title_short |
OsCBE1, a Substrate Receptor of Cullin4-Based E3 Ubiquitin Ligase, Functions as a Regulator of Abiotic Stress Response and Productivity in Rice |
title_full |
OsCBE1, a Substrate Receptor of Cullin4-Based E3 Ubiquitin Ligase, Functions as a Regulator of Abiotic Stress Response and Productivity in Rice |
title_fullStr |
OsCBE1, a Substrate Receptor of Cullin4-Based E3 Ubiquitin Ligase, Functions as a Regulator of Abiotic Stress Response and Productivity in Rice |
title_full_unstemmed |
OsCBE1, a Substrate Receptor of Cullin4-Based E3 Ubiquitin Ligase, Functions as a Regulator of Abiotic Stress Response and Productivity in Rice |
title_sort |
oscbe1, a substrate receptor of cullin4-based e3 ubiquitin ligase, functions as a regulator of abiotic stress response and productivity in rice |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1661-6596 1422-0067 |
publishDate |
2021-03-01 |
description |
Ubiquitination is an important environmental stress response, and E3 ubiquitin ligases play a major role in the process. T-DNA insertion mutants of rice, <i>Oscbe1-1</i>, and <i>Oscbe1-2,</i> were identified through the screening of cold stress tolerance at seedling stage. <i>O</i>s<i>cbe1</i> mutants showed a significantly higher cold stress tolerance in the fresh weight, chlorophyll content, and photosynthetic efficiency than wild type. Molecular prediction showed that <i>OsCBE1</i> (<i>Oryza sativa</i> Cullin4-Based E3 ubiquitin ligase1) encoded a novel substrate receptor of Cullin4-based E3 ubiquitin ligase complex (C4E3). Whereas <i>Oscbe1</i> mutants had fewer panicles and grains than wild type in the paddy field, the overexpression lines of <i>OsCBE1</i> had more panicles and grains, suggesting that <i>OsCBE1</i> is involved in the regulation of both abiotic stress response and development. <i>Oscbe1</i> mutants also showed ABA hypersensitivity during seed germination, suggesting <i>OsCBE1</i> function for the stress response via ABA signaling. In silico analysis of OsCBE1 activity predicted a CCCH-type transcription factor, OsC3H32, as a putative substrate. Co-IP (Co-immunoprecipitation) study showed that OsCBE1 interacts with OsDDB1, an expected binding component of OsCBE1 and OsC3H32. Additionally, expression of <i>OsOLE16, OsOLE18</i>, and <i>OsBURP5</i> were negatively related with expression of <i>OsCBE1</i>. These results suggest that <i>OsCBE1</i> functions as a regulator of the abiotic stress response via CCCH as a member of the C4E3. |
topic |
abiotic stress cullin4 crop productivity E3 ubiquitin ligase rice |
url |
https://www.mdpi.com/1422-0067/22/5/2487 |
work_keys_str_mv |
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